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SLiMSuite SLiMFinder Server

# Output for SLiMFinder V5.2.2: Tue Dec  8 11:13:55 2015
# 1 warnings; 0 errors: see log output (below) for details.
# JobID: 15120800001

Your SLiMFinder job has finished running and outputs have been parsed. Click on tabs to see server output. (Mouseover for description.)

The outfmt tab contains more information on the outputs. Click here for SLiMFinder help/documentation.

Content for individual tabs can be returned using &rest=X, where X is the tab name (e.g. &rest=log). Full output can be returned as text using &rest=full and parsed using SLiMParser.

JobID 15120800001 (slimfinder) Finished.
IP:129.94.146.29
No queue.
slimfinder&uniprotid=LIG_PCNA_PIPBox_1&dismask=T
Run Started: 2015-12-08 11:13:55; PID=35116
Run finished: 2015-12-08 11:16:51

SLiMs and SLiMFinder

Short linear motifs (SLiMs) in proteins are functional microdomains of fundamental importance in many biological
systems. SLiMs typically consist of a 3 to 10 amino acid stretch of the primary protein sequence, of which as few
as two sites may be important for activity. SLiMFinder is a SLiM discovery program building on the principles of
the SLiMDisc software for accounting for evolutionary relationships between input proteins. This stops results
being dominated by motifs shared for reasons of history, rather than function. SLiMFinder runs in two phases:
(1) SLiMBuild constructs the motif search space based on number of defined positions, maximum length of "wildcard
spacers" and allowed amino acid ambiguities; (2) SLiMChance assesses the over-representation of all motifs,
correcting for the size of the SLiMBuild search space. This gives SLiMFinder high specificity.

Protein sequences can be masked prior to SLiMBuild. Disorder masking (using IUPred predictions) is highly
recommended. Other masking options are described in the manual and/or literature.

Running SLiMFinder

The standared REST server call for SLiMFinder is in the form:
slimfinder&uniprotid=LIST&dismask=T/F&consmask=T/F

Run with &rest=docs for program documentation and options. A plain text version is accessed with &rest=help.
&rest=OUTFMT can be used to retrieve individual parts of the output, matching the tabs in the default
(&rest=format) output. Individual OUTFMT elements can also be parsed from the full (&rest=full) server output,
which is formatted as follows:
###~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~###
# OUTFMT:
... contents for OUTFMT section ...


More options are available through the SLiMFinder server: http://www.slimsuite.unsw.edu.au/servers/slimfinder.php

After running, click on the main tab to see overall SLiM predictions. If any SLiMS have been predicted, the
occ tab will have details of which proteins (and where) they occur.

If no SLiMs are returned: [1] Try altering the masking settings. (Disorder masking is recommended. Conservation
masking can sometimes help but it depend on the dataset.) [2] Try relaxing the probability cutoff. Set
[probcut=1.0]{cmd:probcut} to see the best motifs, regardless of significance. (You may also want to reduce the [topranks=X]{cmd:topranks}
setting.)

Available REST Outputs

main = Main results table of predicted SLiM patterns (if any) [[extras=-1]{cmd:extras}]
occ = Occurrence table showing individual SLiM occurrences in input proteins [[extras=0]{cmd:extras}]
upc = List of Unrelated Protein Clusters (UPC) used for evolutionary corrections [[extras=0]{cmd:extras}]
cloud = Predicted SLiM "cloud" output, which groups overlapping motifs [[extras=1]{cmd:extras}]
seqin = Input sequence data [[extras=-1]{cmd:extras}]
slimdb = Parsed input sequences in fasta format, used for UPC generation etc. [[extras=0]{cmd:extras}]
masked = Masked input sequences (masked residues marked with X) [[extras=1]{cmd:extras}]
mapping = Fasta format with positions of SLiM occurrences aligned [[extras=1]{cmd:extras}]
motifaln = Fasta format of individual SLiM alignments (unmasked sequences) [[extras=1]{cmd:extras}]
maskaln = Fasta format of individual SLiM alignments (masked sequences) [[extras=1]{cmd:extras}]

Additional REST Outputs [extras>1]

To get additional REST outputs, set &extras=2 or &extras=3. This may increase run times noticeably,
depending on the number of SLiMs returned.

motifs = SLiM predictions reformatted in plain motif format for CompariMotif [[extras=2]{cmd:extras}]
compare = Results of all-by-all CompariMotif search of predicted SLiMs [[extras=2]{cmd:extras}]
xgmml = SLiMs, occurrences and motif relationships in a Cytoscape-compatible network [[extras=2]{cmd:extras}]
dismatrix = Input sequence distance matrix [[extras=3]{cmd:extras}]
rank = Main table in SLiMDisc output format [[extras=3]{cmd:extras}]
dat.rank = Occurrence table in SLiMDisc output format [[extras=3]{cmd:extras}]
teiresias = Motif prediction output in TEIRESIAS format [[extras=3]{cmd:extras} [teiresias=T]{cmd:teiresias}]
teiresias.fasta = TEIRESIAS masked fasta output [[extras=3]{cmd:extras} [teiresias=T]{cmd:teiresias}]
Dataset,RunID,Masking,Build,Chance,RunTime,SeqNum,UPNum,AANum,MotNum,Rank,Sig,Pattern,IC,Occ,Support,UP,ExpUP,Prob,Cloud,CloudSeq,CloudUP
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,1,3.42e-12,Q..[IL].SFF,4.77,7,7,6,0.002,1.32e-20,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,2,2.87e-11,Q.[ST]..SFF,4.77,7,7,6,0.003,1.11e-19,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,3,6.06e-11,Q.[ST][IL]..FF,4.54,10,10,6,0.004,2.34e-19,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,4,2.64e-10,Q.TL..FF,5.00,5,5,5,9.01e-04,1.02e-18,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,5,8.15e-09,Q..L..FF,4.00,8,8,6,0.016,1.89e-15,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,6,1.11e-08,[ST][IL].SFF,4.54,7,6,6,0.009,4.27e-17,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,7,1.85e-08,TL.SFF,5.00,5,5,5,0.002,7.13e-17,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,8,3.76e-08,Q.[ST][IL].S.F,4.54,6,6,6,0.011,1.45e-16,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,9,4.40e-08,Q.[ST][IL].SF,4.54,6,6,6,0.011,1.70e-16,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,10,9.98e-08,Q..[IL]..FF,3.77,14,14,6,0.025,2.31e-14,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,11,1.55e-06,Q..I..FF..K,5.00,4,4,4,7.69e-04,5.97e-15,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,12,9.24e-06,Q.T..SFF,5.00,4,4,4,0.001,3.56e-14,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,13,1.66e-05,[IL].SFF,3.77,9,8,6,0.058,3.83e-12,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,14,1.88e-05,"TL.{0,1}S.{0,1}FF",5.00,5,5,5,0.008,7.27e-14,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,15,2.05e-05,Q..L.SFF,5.00,5,5,4,0.001,7.90e-14,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,16,2.56e-05,"Q..I..FF.{1,2}K",5.00,5,5,4,0.002,9.88e-14,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,17,4.39e-05,TL..FF,4.00,6,6,5,0.023,1.02e-11,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,18,5.50e-05,Q..[IL].S.F,3.77,8,8,6,0.070,1.27e-11,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,19,6.39e-05,Q..[IL].SF,3.77,7,7,6,0.072,1.48e-11,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,20,1.07e-04,K..Q..[IL]..FF,4.77,4,4,4,0.002,4.14e-13,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,21,1.40e-04,[ST]..SFF,3.77,8,7,6,0.082,3.23e-11,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,22,1.53e-04,[KR]Q..L..FF,4.77,5,5,4,0.002,5.92e-13,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,23,1.64e-04,Q.TL..F,4.00,5,5,5,0.030,3.81e-11,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,24,2.11e-04,Q.TL.S.F,5.00,4,4,4,0.003,8.13e-13,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,25,2.13e-04,T..SFF,4.00,5,5,5,0.031,4.92e-11,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,26,2.33e-04,Q.TL.SF,5.00,4,4,4,0.003,9.00e-13,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,27,2.53e-04,[ST][IL]..FF,3.54,11,10,6,0.091,5.85e-11,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,28,3.68e-04,Q..I..FF,4.00,6,6,4,0.008,8.53e-11,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,29,4.49e-04,Q.[ST]..S.F,3.77,8,8,6,0.100,1.04e-10,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,30,5.03e-04,[KR]..TL..FF,4.77,4,4,4,0.003,1.94e-12,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,31,5.25e-04,Q.[ST]..SF,3.77,7,7,6,0.10,1.22e-10,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,32,5.55e-04,L.SFF,4.00,6,6,5,0.038,1.29e-10,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,33,5.99e-04,Q.T..S.F,4.00,5,5,5,0.038,1.39e-10,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,34,7.21e-04,"I..FF.{1,2}K",4.00,6,6,5,0.040,1.67e-10,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,35,0.001,Q.[ST][IL]..F,3.54,10,10,6,0.12,2.57e-10,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,36,0.002,[KR]Q.TL..F,4.77,4,4,4,0.004,6.89e-12,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,37,0.002,"Q.T.{1,2}S.{0,1}FF",5.00,5,5,4,0.005,8.94e-12,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,38,0.004,[ILM]..F[FY],2.40,20,17,8,0.98,5.27e-08,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,39,0.006,[IL]..FF,2.77,17,16,7,0.59,8.47e-08,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,40,0.010,TL.S.F,4.00,5,5,5,0.067,2.24e-09,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,41,0.011,TL.SF,4.00,5,5,5,0.069,2.57e-09,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,42,0.011,I..FF..K,4.00,4,4,4,0.020,2.57e-09,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,43,0.013,Q.SI..FF,5.00,3,3,3,7.66e-04,4.91e-11,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,44,0.019,"Q.T.{1,2}S.F",4.00,6,6,5,0.077,4.48e-09,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,45,0.020,"Q.T..S.{0,1}F",4.00,5,5,5,0.077,4.58e-09,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,46,0.026,L..FF,3.00,9,9,6,0.39,3.61e-07,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,47,0.037,[ILMV]..F[FY],2.31,22,18,8,1.31,5.20e-07,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,48,0.048,I..FF,3.00,8,8,5,0.21,6.84e-07,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,49,0.093,KQ..L..FF,5.00,3,3,3,0.002,3.75e-10,1,18,8
slimfinder,15120800001,FreqDisComp-5-8FT,l5w2o2a3,Sig,00:02:48,18,8,8004,50,50,0.098,Q..L..F,3.00,8,8,6,0.50,1.43e-06,1,18,8
Dataset,RunID,Rank,Pattern,Sig,Seq,Start_Pos,End_Pos,Prot_Len,Match,Variant,MisMatch,Desc,PepSeq,PepDesign
slimfinder,15120800001,1,Q..[IL].SFF,3.42e-12,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q..[IL].SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,1,Q..[IL].SFF,3.42e-12,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q..[IL].SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,1,Q..[IL].SFF,3.42e-12,DPOD3_SCHPO__P30261,362,369,372,QKSIMSFF,Q..[IL].SFF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFF,OK
slimfinder,15120800001,1,Q..[IL].SFF,3.42e-12,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q..[IL].SFF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,1,Q..[IL].SFF,3.42e-12,MSH6_YEAST__Q03834,27,34,1242,QSSLLSFF,Q..[IL].SFF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,QSSLLSFF,OK
slimfinder,15120800001,1,Q..[IL].SFF,3.42e-12,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q..[IL].SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,1,Q..[IL].SFF,3.42e-12,DNLI1_HUMAN__P18858,2,9,919,QRSIMSFF,Q..[IL].SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSFF,OK
slimfinder,15120800001,2,Q.[ST]..SFF,2.87e-11,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q.[ST]..SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,2,Q.[ST]..SFF,2.87e-11,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q.[ST]..SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,2,Q.[ST]..SFF,2.87e-11,DPOD3_SCHPO__P30261,362,369,372,QKSIMSFF,Q.[ST]..SFF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFF,OK
slimfinder,15120800001,2,Q.[ST]..SFF,2.87e-11,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q.[ST]..SFF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,2,Q.[ST]..SFF,2.87e-11,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q.[ST]..SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,2,Q.[ST]..SFF,2.87e-11,MSH6_YEAST__Q03834,27,34,1242,QSSLLSFF,Q.[ST]..SFF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,QSSLLSFF,OK
slimfinder,15120800001,2,Q.[ST]..SFF,2.87e-11,DNLI1_HUMAN__P18858,2,9,919,QRSIMSFF,Q.[ST]..SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSFF,OK
slimfinder,15120800001,3,Q.[ST][IL]..FF,6.06e-11,DPOD3_HUMAN__Q15054,456,463,466,QVSITGFF,Q.[ST][IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,QVSITGFF,OK
slimfinder,15120800001,3,Q.[ST][IL]..FF,6.06e-11,MSH3_YEAST__P25336,4,11,1018,QPTISRFF,Q.[ST][IL]..FF,0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,QPTISRFF,OK
slimfinder,15120800001,3,Q.[ST][IL]..FF,6.06e-11,DPOD3_SCHPO__P30261,362,369,372,QKSIMSFF,Q.[ST][IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFF,OK
slimfinder,15120800001,3,Q.[ST][IL]..FF,6.06e-11,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q.[ST][IL]..FF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,3,Q.[ST][IL]..FF,6.06e-11,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q.[ST][IL]..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,3,Q.[ST][IL]..FF,6.06e-11,DNLI1_YEAST__P04819,38,45,755,QATLARFF,Q.[ST][IL]..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,QATLARFF,OK
slimfinder,15120800001,3,Q.[ST][IL]..FF,6.06e-11,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q.[ST][IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,3,Q.[ST][IL]..FF,6.06e-11,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q.[ST][IL]..FF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,3,Q.[ST][IL]..FF,6.06e-11,UNG_YEAST__P12887,21,28,359,QTTIEDFF,Q.[ST][IL]..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,QTTIEDFF,OK
slimfinder,15120800001,3,Q.[ST][IL]..FF,6.06e-11,DNLI1_HUMAN__P18858,2,9,919,QRSIMSFF,Q.[ST][IL]..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSFF,OK
slimfinder,15120800001,4,Q.TL..FF,2.64e-10,DNLI1_YEAST__P04819,38,45,755,QATLARFF,Q.TL..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,QATLARFF,OK
slimfinder,15120800001,4,Q.TL..FF,2.64e-10,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q.TL..FF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,4,Q.TL..FF,2.64e-10,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q.TL..FF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,4,Q.TL..FF,2.64e-10,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q.TL..FF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,4,Q.TL..FF,2.64e-10,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q.TL..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,5,Q..L..FF,8.15e-09,DNLI1_YEAST__P04819,38,45,755,QATLARFF,Q..L..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,QATLARFF,OK
slimfinder,15120800001,5,Q..L..FF,8.15e-09,FEN1_YEAST__P26793,340,347,382,QGRLDGFF,Q..L..FF,0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;,QGRLDGFF,Warning: DG
slimfinder,15120800001,5,Q..L..FF,8.15e-09,FEN1_HUMAN__P39748,337,344,380,QGRLDDFF,Q..L..FF,0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;,QGRLDDFF,OK
slimfinder,15120800001,5,Q..L..FF,8.15e-09,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q..L..FF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,5,Q..L..FF,8.15e-09,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q..L..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,5,Q..L..FF,8.15e-09,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q..L..FF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,5,Q..L..FF,8.15e-09,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q..L..FF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,5,Q..L..FF,8.15e-09,MSH6_YEAST__Q03834,27,34,1242,QSSLLSFF,Q..L..FF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,QSSLLSFF,OK
slimfinder,15120800001,6,[ST][IL].SFF,1.11e-08,RRM3_YEAST__P38766,37,42,723,TLSSFF,[ST][IL].SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,TLSSFF,OK
slimfinder,15120800001,6,[ST][IL].SFF,1.11e-08,UNG_HUMAN__P13051,6,11,313,TLYSFF,[ST][IL].SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,TLYSFF,OK
slimfinder,15120800001,6,[ST][IL].SFF,1.11e-08,DPOD3_SCHPO__P30261,364,369,372,SIMSFF,[ST][IL].SFF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,SIMSFF,OK
slimfinder,15120800001,6,[ST][IL].SFF,1.11e-08,DPOD3_YEAST__P47110,340,345,350,TLESFF,[ST][IL].SFF,0,RecName: Full=DNA polymerase delta subunit 3;,TLESFF,OK
slimfinder,15120800001,6,[ST][IL].SFF,1.11e-08,MSH6_HUMAN__P52701,6,11,1360,TLYSFF,[ST][IL].SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,TLYSFF,OK
slimfinder,15120800001,6,[ST][IL].SFF,1.11e-08,DNLI1_HUMAN__P18858,4,9,919,SIMSFF,[ST][IL].SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,SIMSFF,OK
slimfinder,15120800001,6,[ST][IL].SFF,1.11e-08,DNLI1_HUMAN__P18858,227,232,919,TLSSFF,[ST][IL].SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,TLSSFF,OK
slimfinder,15120800001,7,TL.SFF,1.85e-08,DNLI1_HUMAN__P18858,227,232,919,TLSSFF,TL.SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,TLSSFF,OK
slimfinder,15120800001,7,TL.SFF,1.85e-08,DPOD3_YEAST__P47110,340,345,350,TLESFF,TL.SFF,0,RecName: Full=DNA polymerase delta subunit 3;,TLESFF,OK
slimfinder,15120800001,7,TL.SFF,1.85e-08,RRM3_YEAST__P38766,37,42,723,TLSSFF,TL.SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,TLSSFF,OK
slimfinder,15120800001,7,TL.SFF,1.85e-08,MSH6_HUMAN__P52701,6,11,1360,TLYSFF,TL.SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,TLYSFF,OK
slimfinder,15120800001,7,TL.SFF,1.85e-08,UNG_HUMAN__P13051,6,11,313,TLYSFF,TL.SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,TLYSFF,OK
slimfinder,15120800001,8,Q.[ST][IL].S.F,3.76e-08,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q.[ST][IL].S.F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,8,Q.[ST][IL].S.F,3.76e-08,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q.[ST][IL].S.F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,8,Q.[ST][IL].S.F,3.76e-08,DPOD3_SCHPO__P30261,362,369,372,QKSIMSFF,Q.[ST][IL].S.F,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFF,OK
slimfinder,15120800001,8,Q.[ST][IL].S.F,3.76e-08,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q.[ST][IL].S.F,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,8,Q.[ST][IL].S.F,3.76e-08,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q.[ST][IL].S.F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,8,Q.[ST][IL].S.F,3.76e-08,DNLI1_HUMAN__P18858,2,9,919,QRSIMSFF,Q.[ST][IL].S.F,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSFF,OK
slimfinder,15120800001,9,Q.[ST][IL].SF,4.40e-08,RRM3_YEAST__P38766,35,41,723,QQTLSSF,Q.[ST][IL].SF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSF,OK
slimfinder,15120800001,9,Q.[ST][IL].SF,4.40e-08,UNG_HUMAN__P13051,4,10,313,QKTLYSF,Q.[ST][IL].SF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSF,OK
slimfinder,15120800001,9,Q.[ST][IL].SF,4.40e-08,DPOD3_SCHPO__P30261,362,368,372,QKSIMSF,Q.[ST][IL].SF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSF,OK
slimfinder,15120800001,9,Q.[ST][IL].SF,4.40e-08,DPOD3_YEAST__P47110,338,344,350,QGTLESF,Q.[ST][IL].SF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESF,OK
slimfinder,15120800001,9,Q.[ST][IL].SF,4.40e-08,MSH6_HUMAN__P52701,4,10,1360,QSTLYSF,Q.[ST][IL].SF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSF,OK
slimfinder,15120800001,9,Q.[ST][IL].SF,4.40e-08,DNLI1_HUMAN__P18858,2,8,919,QRSIMSF,Q.[ST][IL].SF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,DPOD3_HUMAN__Q15054,456,463,466,QVSITGFF,Q..[IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,QVSITGFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,MSH3_YEAST__P25336,4,11,1018,QPTISRFF,Q..[IL]..FF,0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,QPTISRFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q..[IL]..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,FEN1_YEAST__P26793,340,347,382,QGRLDGFF,Q..[IL]..FF,0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;,QGRLDGFF,Warning: DG
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,DPOD3_SCHPO__P30261,362,369,372,QKSIMSFF,Q..[IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q..[IL]..FF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,FEN1_HUMAN__P39748,337,344,380,QGRLDDFF,Q..[IL]..FF,0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;,QGRLDDFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,DNLI1_YEAST__P04819,38,45,755,QATLARFF,Q..[IL]..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,QATLARFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q..[IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q..[IL]..FF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,MSH6_YEAST__Q03834,27,34,1242,QSSLLSFF,Q..[IL]..FF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,QSSLLSFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,UNG_YEAST__P12887,21,28,359,QTTIEDFF,Q..[IL]..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,QTTIEDFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,RAD2_YEAST__P07276,995,1002,1031,QKRINEFF,Q..[IL]..FF,0,RecName: Full=DNA repair protein RAD2; EC=3.1.-.-;,QKRINEFF,OK
slimfinder,15120800001,10,Q..[IL]..FF,9.98e-08,DNLI1_HUMAN__P18858,2,9,919,QRSIMSFF,Q..[IL]..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSFF,OK
slimfinder,15120800001,11,Q..I..FF..K,1.55e-06,DNLI1_HUMAN__P18858,2,12,919,QRSIMSFFHPK,Q..I..FF..K,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSFFHPK,OK
slimfinder,15120800001,11,Q..I..FF..K,1.55e-06,DPOD3_HUMAN__Q15054,456,466,466,QVSITGFFQRK,Q..I..FF..K,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,QVSITGFFQRK,OK
slimfinder,15120800001,11,Q..I..FF..K,1.55e-06,UNG_YEAST__P12887,21,31,359,QTTIEDFFGTK,Q..I..FF..K,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,QTTIEDFFGTK,OK
slimfinder,15120800001,11,Q..I..FF..K,1.55e-06,DPOD3_SCHPO__P30261,362,372,372,QKSIMSFFGKK,Q..I..FF..K,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFFGKK,OK
slimfinder,15120800001,12,Q.T..SFF,9.24e-06,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q.T..SFF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,12,Q.T..SFF,9.24e-06,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q.T..SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,12,Q.T..SFF,9.24e-06,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q.T..SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,12,Q.T..SFF,9.24e-06,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q.T..SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,13,[IL].SFF,1.66e-05,ERCC5_HUMAN__P28715,993,997,1186,IDSFF,[IL].SFF,0,RecName: Full=DNA repair protein complementing XP-G cells; EC=3.1.-.-; AltName: Full=DNA excision repair protein ERCC-5; AltName: Full=Xeroderma pigmentosum group G-complementing protein;,IDSFF,OK
slimfinder,15120800001,13,[IL].SFF,1.66e-05,RRM3_YEAST__P38766,38,42,723,LSSFF,[IL].SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,LSSFF,OK
slimfinder,15120800001,13,[IL].SFF,1.66e-05,UNG_HUMAN__P13051,7,11,313,LYSFF,[IL].SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,LYSFF,OK
slimfinder,15120800001,13,[IL].SFF,1.66e-05,DPOD3_SCHPO__P30261,365,369,372,IMSFF,[IL].SFF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,IMSFF,OK
slimfinder,15120800001,13,[IL].SFF,1.66e-05,DPOD3_YEAST__P47110,341,345,350,LESFF,[IL].SFF,0,RecName: Full=DNA polymerase delta subunit 3;,LESFF,OK
slimfinder,15120800001,13,[IL].SFF,1.66e-05,MSH6_YEAST__Q03834,30,34,1242,LLSFF,[IL].SFF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,LLSFF,OK
slimfinder,15120800001,13,[IL].SFF,1.66e-05,MSH6_HUMAN__P52701,7,11,1360,LYSFF,[IL].SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,LYSFF,OK
slimfinder,15120800001,13,[IL].SFF,1.66e-05,DNLI1_HUMAN__P18858,5,9,919,IMSFF,[IL].SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,IMSFF,OK
slimfinder,15120800001,13,[IL].SFF,1.66e-05,DNLI1_HUMAN__P18858,228,232,919,LSSFF,[IL].SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,LSSFF,OK
slimfinder,15120800001,14,"TL.{0,1}S.{0,1}FF",1.88e-05,DNLI1_HUMAN__P18858,227,232,919,TLSSFF,TL.SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,TLSSFF,OK
slimfinder,15120800001,14,"TL.{0,1}S.{0,1}FF",1.88e-05,RRM3_YEAST__P38766,37,42,723,TLSSFF,TL.SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,TLSSFF,OK
slimfinder,15120800001,14,"TL.{0,1}S.{0,1}FF",1.88e-05,MSH6_HUMAN__P52701,6,11,1360,TLYSFF,TL.SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,TLYSFF,OK
slimfinder,15120800001,14,"TL.{0,1}S.{0,1}FF",1.88e-05,DPOD3_YEAST__P47110,340,345,350,TLESFF,TL.SFF,0,RecName: Full=DNA polymerase delta subunit 3;,TLESFF,OK
slimfinder,15120800001,14,"TL.{0,1}S.{0,1}FF",1.88e-05,UNG_HUMAN__P13051,6,11,313,TLYSFF,TL.SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,TLYSFF,OK
slimfinder,15120800001,15,Q..L.SFF,2.05e-05,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q..L.SFF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,15,Q..L.SFF,2.05e-05,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q..L.SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,15,Q..L.SFF,2.05e-05,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q..L.SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,15,Q..L.SFF,2.05e-05,MSH6_YEAST__Q03834,27,34,1242,QSSLLSFF,Q..L.SFF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,QSSLLSFF,OK
slimfinder,15120800001,15,Q..L.SFF,2.05e-05,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q..L.SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,16,"Q..I..FF.{1,2}K",2.56e-05,DPOD3_SCHPO__P30261,362,371,372,QKSIMSFFGK,Q..I..FF.K,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFFGK,OK
slimfinder,15120800001,16,"Q..I..FF.{1,2}K",2.56e-05,DPOD3_SCHPO__P30261,362,372,372,QKSIMSFFGKK,Q..I..FF..K,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFFGKK,OK
slimfinder,15120800001,16,"Q..I..FF.{1,2}K",2.56e-05,MSH3_YEAST__P25336,4,13,1018,QPTISRFFKK,Q..I..FF.K,0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,QPTISRFFKK,OK
slimfinder,15120800001,16,"Q..I..FF.{1,2}K",2.56e-05,UNG_YEAST__P12887,21,31,359,QTTIEDFFGTK,Q..I..FF..K,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,QTTIEDFFGTK,OK
slimfinder,15120800001,16,"Q..I..FF.{1,2}K",2.56e-05,DPOD3_HUMAN__Q15054,456,466,466,QVSITGFFQRK,Q..I..FF..K,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,QVSITGFFQRK,OK
slimfinder,15120800001,16,"Q..I..FF.{1,2}K",2.56e-05,DNLI1_HUMAN__P18858,2,12,919,QRSIMSFFHPK,Q..I..FF..K,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSFFHPK,OK
slimfinder,15120800001,17,TL..FF,4.39e-05,RRM3_YEAST__P38766,37,42,723,TLSSFF,TL..FF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,TLSSFF,OK
slimfinder,15120800001,17,TL..FF,4.39e-05,UNG_HUMAN__P13051,6,11,313,TLYSFF,TL..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,TLYSFF,OK
slimfinder,15120800001,17,TL..FF,4.39e-05,DNLI1_YEAST__P04819,40,45,755,TLARFF,TL..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,TLARFF,OK
slimfinder,15120800001,17,TL..FF,4.39e-05,DPOD3_YEAST__P47110,340,345,350,TLESFF,TL..FF,0,RecName: Full=DNA polymerase delta subunit 3;,TLESFF,OK
slimfinder,15120800001,17,TL..FF,4.39e-05,MSH6_HUMAN__P52701,6,11,1360,TLYSFF,TL..FF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,TLYSFF,OK
slimfinder,15120800001,17,TL..FF,4.39e-05,DNLI1_HUMAN__P18858,227,232,919,TLSSFF,TL..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,TLSSFF,OK
slimfinder,15120800001,18,Q..[IL].S.F,5.50e-05,DPOD3_SCHPO__P30261,362,369,372,QKSIMSFF,Q..[IL].S.F,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFF,OK
slimfinder,15120800001,18,Q..[IL].S.F,5.50e-05,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q..[IL].S.F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,18,Q..[IL].S.F,5.50e-05,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q..[IL].S.F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,18,Q..[IL].S.F,5.50e-05,DNMT1_HUMAN__P26358,164,171,1616,QTTITSHF,Q..[IL].S.F,0,RecName: Full=DNA (cytosine-5)-methyltransferase 1; Short=Dnmt1; EC=2.1.1.37; AltName: Full=CXXC-type zinc finger protein 9; AltName: Full=DNA methyltransferase HsaI; Short=DNA MTase HsaI; Short=M.HsaI; AltName: Full=MCMT;,QTTITSHF,OK
slimfinder,15120800001,18,Q..[IL].S.F,5.50e-05,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q..[IL].S.F,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,18,Q..[IL].S.F,5.50e-05,MSH6_YEAST__Q03834,27,34,1242,QSSLLSFF,Q..[IL].S.F,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,QSSLLSFF,OK
slimfinder,15120800001,18,Q..[IL].S.F,5.50e-05,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q..[IL].S.F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,18,Q..[IL].S.F,5.50e-05,DNLI1_HUMAN__P18858,2,9,919,QRSIMSFF,Q..[IL].S.F,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSFF,OK
slimfinder,15120800001,19,Q..[IL].SF,6.39e-05,RRM3_YEAST__P38766,35,41,723,QQTLSSF,Q..[IL].SF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSF,OK
slimfinder,15120800001,19,Q..[IL].SF,6.39e-05,UNG_HUMAN__P13051,4,10,313,QKTLYSF,Q..[IL].SF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSF,OK
slimfinder,15120800001,19,Q..[IL].SF,6.39e-05,DPOD3_SCHPO__P30261,362,368,372,QKSIMSF,Q..[IL].SF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSF,OK
slimfinder,15120800001,19,Q..[IL].SF,6.39e-05,DPOD3_YEAST__P47110,338,344,350,QGTLESF,Q..[IL].SF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESF,OK
slimfinder,15120800001,19,Q..[IL].SF,6.39e-05,MSH6_YEAST__Q03834,27,33,1242,QSSLLSF,Q..[IL].SF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,QSSLLSF,OK
slimfinder,15120800001,19,Q..[IL].SF,6.39e-05,MSH6_HUMAN__P52701,4,10,1360,QSTLYSF,Q..[IL].SF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSF,OK
slimfinder,15120800001,19,Q..[IL].SF,6.39e-05,DNLI1_HUMAN__P18858,2,8,919,QRSIMSF,Q..[IL].SF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSF,OK
slimfinder,15120800001,20,K..Q..[IL]..FF,1.07e-04,DPOD3_SCHPO__P30261,359,369,372,KPQQKSIMSFF,K..Q..[IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,KPQQKSIMSFF,OK
slimfinder,15120800001,20,K..Q..[IL]..FF,1.07e-04,UNG_YEAST__P12887,18,28,359,KRKQTTIEDFF,K..Q..[IL]..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,KRKQTTIEDFF,OK
slimfinder,15120800001,20,K..Q..[IL]..FF,1.07e-04,DNLI1_YEAST__P04819,35,45,755,KPKQATLARFF,K..Q..[IL]..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,KPKQATLARFF,OK
slimfinder,15120800001,20,K..Q..[IL]..FF,1.07e-04,MSH6_YEAST__Q03834,24,34,1242,KMKQSSLLSFF,K..Q..[IL]..FF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,KMKQSSLLSFF,OK
slimfinder,15120800001,21,[ST]..SFF,1.40e-04,RRM3_YEAST__P38766,37,42,723,TLSSFF,[ST]..SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,TLSSFF,OK
slimfinder,15120800001,21,[ST]..SFF,1.40e-04,UNG_HUMAN__P13051,6,11,313,TLYSFF,[ST]..SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,TLYSFF,OK
slimfinder,15120800001,21,[ST]..SFF,1.40e-04,DPOD3_SCHPO__P30261,364,369,372,SIMSFF,[ST]..SFF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,SIMSFF,OK
slimfinder,15120800001,21,[ST]..SFF,1.40e-04,DPOD3_YEAST__P47110,340,345,350,TLESFF,[ST]..SFF,0,RecName: Full=DNA polymerase delta subunit 3;,TLESFF,OK
slimfinder,15120800001,21,[ST]..SFF,1.40e-04,MSH6_HUMAN__P52701,6,11,1360,TLYSFF,[ST]..SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,TLYSFF,OK
slimfinder,15120800001,21,[ST]..SFF,1.40e-04,MSH6_YEAST__Q03834,29,34,1242,SLLSFF,[ST]..SFF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,SLLSFF,OK
slimfinder,15120800001,21,[ST]..SFF,1.40e-04,DNLI1_HUMAN__P18858,4,9,919,SIMSFF,[ST]..SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,SIMSFF,OK
slimfinder,15120800001,21,[ST]..SFF,1.40e-04,DNLI1_HUMAN__P18858,227,232,919,TLSSFF,[ST]..SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,TLSSFF,OK
slimfinder,15120800001,22,[KR]Q..L..FF,1.53e-04,DNLI1_YEAST__P04819,37,45,755,KQATLARFF,[KR]Q..L..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,KQATLARFF,OK
slimfinder,15120800001,22,[KR]Q..L..FF,1.53e-04,DPOD3_YEAST__P47110,337,345,350,KQGTLESFF,[KR]Q..L..FF,0,RecName: Full=DNA polymerase delta subunit 3;,KQGTLESFF,OK
slimfinder,15120800001,22,[KR]Q..L..FF,1.53e-04,RRM3_YEAST__P38766,34,42,723,RQQTLSSFF,[KR]Q..L..FF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,RQQTLSSFF,OK
slimfinder,15120800001,22,[KR]Q..L..FF,1.53e-04,MSH6_YEAST__Q03834,26,34,1242,KQSSLLSFF,[KR]Q..L..FF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,KQSSLLSFF,OK
slimfinder,15120800001,22,[KR]Q..L..FF,1.53e-04,MSH6_HUMAN__P52701,3,11,1360,RQSTLYSFF,[KR]Q..L..FF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,RQSTLYSFF,OK
slimfinder,15120800001,23,Q.TL..F,1.64e-04,DNLI1_YEAST__P04819,38,44,755,QATLARF,Q.TL..F,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,QATLARF,OK
slimfinder,15120800001,23,Q.TL..F,1.64e-04,DPOD3_YEAST__P47110,338,344,350,QGTLESF,Q.TL..F,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESF,OK
slimfinder,15120800001,23,Q.TL..F,1.64e-04,RRM3_YEAST__P38766,35,41,723,QQTLSSF,Q.TL..F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSF,OK
slimfinder,15120800001,23,Q.TL..F,1.64e-04,MSH6_HUMAN__P52701,4,10,1360,QSTLYSF,Q.TL..F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSF,OK
slimfinder,15120800001,23,Q.TL..F,1.64e-04,UNG_HUMAN__P13051,4,10,313,QKTLYSF,Q.TL..F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSF,OK
slimfinder,15120800001,24,Q.TL.S.F,2.11e-04,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q.TL.S.F,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,24,Q.TL.S.F,2.11e-04,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q.TL.S.F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,24,Q.TL.S.F,2.11e-04,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q.TL.S.F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,24,Q.TL.S.F,2.11e-04,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q.TL.S.F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,25,T..SFF,2.13e-04,DNLI1_HUMAN__P18858,227,232,919,TLSSFF,T..SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,TLSSFF,OK
slimfinder,15120800001,25,T..SFF,2.13e-04,DPOD3_YEAST__P47110,340,345,350,TLESFF,T..SFF,0,RecName: Full=DNA polymerase delta subunit 3;,TLESFF,OK
slimfinder,15120800001,25,T..SFF,2.13e-04,RRM3_YEAST__P38766,37,42,723,TLSSFF,T..SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,TLSSFF,OK
slimfinder,15120800001,25,T..SFF,2.13e-04,MSH6_HUMAN__P52701,6,11,1360,TLYSFF,T..SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,TLYSFF,OK
slimfinder,15120800001,25,T..SFF,2.13e-04,UNG_HUMAN__P13051,6,11,313,TLYSFF,T..SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,TLYSFF,OK
slimfinder,15120800001,26,Q.TL.SF,2.33e-04,DPOD3_YEAST__P47110,338,344,350,QGTLESF,Q.TL.SF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESF,OK
slimfinder,15120800001,26,Q.TL.SF,2.33e-04,MSH6_HUMAN__P52701,4,10,1360,QSTLYSF,Q.TL.SF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSF,OK
slimfinder,15120800001,26,Q.TL.SF,2.33e-04,RRM3_YEAST__P38766,35,41,723,QQTLSSF,Q.TL.SF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSF,OK
slimfinder,15120800001,26,Q.TL.SF,2.33e-04,UNG_HUMAN__P13051,4,10,313,QKTLYSF,Q.TL.SF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSF,OK
slimfinder,15120800001,27,[ST][IL]..FF,2.53e-04,DPOD3_HUMAN__Q15054,458,463,466,SITGFF,[ST][IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,SITGFF,OK
slimfinder,15120800001,27,[ST][IL]..FF,2.53e-04,MSH3_YEAST__P25336,6,11,1018,TISRFF,[ST][IL]..FF,0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,TISRFF,OK
slimfinder,15120800001,27,[ST][IL]..FF,2.53e-04,DPOD3_SCHPO__P30261,364,369,372,SIMSFF,[ST][IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,SIMSFF,OK
slimfinder,15120800001,27,[ST][IL]..FF,2.53e-04,RRM3_YEAST__P38766,37,42,723,TLSSFF,[ST][IL]..FF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,TLSSFF,OK
slimfinder,15120800001,27,[ST][IL]..FF,2.53e-04,UNG_HUMAN__P13051,6,11,313,TLYSFF,[ST][IL]..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,TLYSFF,OK
slimfinder,15120800001,27,[ST][IL]..FF,2.53e-04,DNLI1_YEAST__P04819,40,45,755,TLARFF,[ST][IL]..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,TLARFF,OK
slimfinder,15120800001,27,[ST][IL]..FF,2.53e-04,DPOD3_YEAST__P47110,340,345,350,TLESFF,[ST][IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3;,TLESFF,OK
slimfinder,15120800001,27,[ST][IL]..FF,2.53e-04,MSH6_HUMAN__P52701,6,11,1360,TLYSFF,[ST][IL]..FF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,TLYSFF,OK
slimfinder,15120800001,27,[ST][IL]..FF,2.53e-04,UNG_YEAST__P12887,23,28,359,TIEDFF,[ST][IL]..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,TIEDFF,OK
slimfinder,15120800001,27,[ST][IL]..FF,2.53e-04,DNLI1_HUMAN__P18858,4,9,919,SIMSFF,[ST][IL]..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,SIMSFF,OK
slimfinder,15120800001,27,[ST][IL]..FF,2.53e-04,DNLI1_HUMAN__P18858,227,232,919,TLSSFF,[ST][IL]..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,TLSSFF,OK
slimfinder,15120800001,28,Q..I..FF,3.68e-04,MSH3_YEAST__P25336,4,11,1018,QPTISRFF,Q..I..FF,0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,QPTISRFF,OK
slimfinder,15120800001,28,Q..I..FF,3.68e-04,DPOD3_SCHPO__P30261,362,369,372,QKSIMSFF,Q..I..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFF,OK
slimfinder,15120800001,28,Q..I..FF,3.68e-04,DPOD3_HUMAN__Q15054,456,463,466,QVSITGFF,Q..I..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,QVSITGFF,OK
slimfinder,15120800001,28,Q..I..FF,3.68e-04,UNG_YEAST__P12887,21,28,359,QTTIEDFF,Q..I..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,QTTIEDFF,OK
slimfinder,15120800001,28,Q..I..FF,3.68e-04,RAD2_YEAST__P07276,995,1002,1031,QKRINEFF,Q..I..FF,0,RecName: Full=DNA repair protein RAD2; EC=3.1.-.-;,QKRINEFF,OK
slimfinder,15120800001,28,Q..I..FF,3.68e-04,DNLI1_HUMAN__P18858,2,9,919,QRSIMSFF,Q..I..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSFF,OK
slimfinder,15120800001,29,Q.[ST]..S.F,4.49e-04,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q.[ST]..S.F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,29,Q.[ST]..S.F,4.49e-04,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q.[ST]..S.F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,29,Q.[ST]..S.F,4.49e-04,DPOD3_SCHPO__P30261,362,369,372,QKSIMSFF,Q.[ST]..S.F,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFF,OK
slimfinder,15120800001,29,Q.[ST]..S.F,4.49e-04,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q.[ST]..S.F,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,29,Q.[ST]..S.F,4.49e-04,DNMT1_HUMAN__P26358,164,171,1616,QTTITSHF,Q.[ST]..S.F,0,RecName: Full=DNA (cytosine-5)-methyltransferase 1; Short=Dnmt1; EC=2.1.1.37; AltName: Full=CXXC-type zinc finger protein 9; AltName: Full=DNA methyltransferase HsaI; Short=DNA MTase HsaI; Short=M.HsaI; AltName: Full=MCMT;,QTTITSHF,OK
slimfinder,15120800001,29,Q.[ST]..S.F,4.49e-04,MSH6_YEAST__Q03834,27,34,1242,QSSLLSFF,Q.[ST]..S.F,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,QSSLLSFF,OK
slimfinder,15120800001,29,Q.[ST]..S.F,4.49e-04,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q.[ST]..S.F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,29,Q.[ST]..S.F,4.49e-04,DNLI1_HUMAN__P18858,2,9,919,QRSIMSFF,Q.[ST]..S.F,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSFF,OK
slimfinder,15120800001,30,[KR]..TL..FF,5.03e-04,DNLI1_YEAST__P04819,37,45,755,KQATLARFF,[KR]..TL..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,KQATLARFF,OK
slimfinder,15120800001,30,[KR]..TL..FF,5.03e-04,DPOD3_YEAST__P47110,337,345,350,KQGTLESFF,[KR]..TL..FF,0,RecName: Full=DNA polymerase delta subunit 3;,KQGTLESFF,OK
slimfinder,15120800001,30,[KR]..TL..FF,5.03e-04,RRM3_YEAST__P38766,34,42,723,RQQTLSSFF,[KR]..TL..FF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,RQQTLSSFF,OK
slimfinder,15120800001,30,[KR]..TL..FF,5.03e-04,MSH6_HUMAN__P52701,3,11,1360,RQSTLYSFF,[KR]..TL..FF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,RQSTLYSFF,OK
slimfinder,15120800001,31,Q.[ST]..SF,5.25e-04,RRM3_YEAST__P38766,35,41,723,QQTLSSF,Q.[ST]..SF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSF,OK
slimfinder,15120800001,31,Q.[ST]..SF,5.25e-04,UNG_HUMAN__P13051,4,10,313,QKTLYSF,Q.[ST]..SF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSF,OK
slimfinder,15120800001,31,Q.[ST]..SF,5.25e-04,DPOD3_SCHPO__P30261,362,368,372,QKSIMSF,Q.[ST]..SF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSF,OK
slimfinder,15120800001,31,Q.[ST]..SF,5.25e-04,DPOD3_YEAST__P47110,338,344,350,QGTLESF,Q.[ST]..SF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESF,OK
slimfinder,15120800001,31,Q.[ST]..SF,5.25e-04,MSH6_HUMAN__P52701,4,10,1360,QSTLYSF,Q.[ST]..SF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSF,OK
slimfinder,15120800001,31,Q.[ST]..SF,5.25e-04,MSH6_YEAST__Q03834,27,33,1242,QSSLLSF,Q.[ST]..SF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,QSSLLSF,OK
slimfinder,15120800001,31,Q.[ST]..SF,5.25e-04,DNLI1_HUMAN__P18858,2,8,919,QRSIMSF,Q.[ST]..SF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSF,OK
slimfinder,15120800001,32,L.SFF,5.55e-04,RRM3_YEAST__P38766,38,42,723,LSSFF,L.SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,LSSFF,OK
slimfinder,15120800001,32,L.SFF,5.55e-04,UNG_HUMAN__P13051,7,11,313,LYSFF,L.SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,LYSFF,OK
slimfinder,15120800001,32,L.SFF,5.55e-04,DPOD3_YEAST__P47110,341,345,350,LESFF,L.SFF,0,RecName: Full=DNA polymerase delta subunit 3;,LESFF,OK
slimfinder,15120800001,32,L.SFF,5.55e-04,MSH6_HUMAN__P52701,7,11,1360,LYSFF,L.SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,LYSFF,OK
slimfinder,15120800001,32,L.SFF,5.55e-04,MSH6_YEAST__Q03834,30,34,1242,LLSFF,L.SFF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,LLSFF,OK
slimfinder,15120800001,32,L.SFF,5.55e-04,DNLI1_HUMAN__P18858,228,232,919,LSSFF,L.SFF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,LSSFF,OK
slimfinder,15120800001,33,Q.T..S.F,5.99e-04,DNMT1_HUMAN__P26358,164,171,1616,QTTITSHF,Q.T..S.F,0,RecName: Full=DNA (cytosine-5)-methyltransferase 1; Short=Dnmt1; EC=2.1.1.37; AltName: Full=CXXC-type zinc finger protein 9; AltName: Full=DNA methyltransferase HsaI; Short=DNA MTase HsaI; Short=M.HsaI; AltName: Full=MCMT;,QTTITSHF,OK
slimfinder,15120800001,33,Q.T..S.F,5.99e-04,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q.T..S.F,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,33,Q.T..S.F,5.99e-04,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q.T..S.F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,33,Q.T..S.F,5.99e-04,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q.T..S.F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,33,Q.T..S.F,5.99e-04,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q.T..S.F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,34,"I..FF.{1,2}K",7.21e-04,MSH3_YEAST__P25336,7,13,1018,ISRFFKK,I..FF.K,0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,ISRFFKK,OK
slimfinder,15120800001,34,"I..FF.{1,2}K",7.21e-04,DPOD3_SCHPO__P30261,365,371,372,IMSFFGK,I..FF.K,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,IMSFFGK,OK
slimfinder,15120800001,34,"I..FF.{1,2}K",7.21e-04,DPOD3_SCHPO__P30261,365,372,372,IMSFFGKK,I..FF..K,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,IMSFFGKK,OK
slimfinder,15120800001,34,"I..FF.{1,2}K",7.21e-04,RFC1_YEAST__P38630,4,10,861,ISDFFGK,I..FF.K,0,RecName: Full=Replication factor C subunit 1; Short=Replication factor C1; AltName: Full=Activator 1 95 kDa subunit; AltName: Full=Cell division control protein 44;,ISDFFGK,OK
slimfinder,15120800001,34,"I..FF.{1,2}K",7.21e-04,DPOD3_HUMAN__Q15054,459,466,466,ITGFFQRK,I..FF..K,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,ITGFFQRK,OK
slimfinder,15120800001,34,"I..FF.{1,2}K",7.21e-04,UNG_YEAST__P12887,24,31,359,IEDFFGTK,I..FF..K,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,IEDFFGTK,OK
slimfinder,15120800001,34,"I..FF.{1,2}K",7.21e-04,DNLI1_HUMAN__P18858,5,12,919,IMSFFHPK,I..FF..K,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,IMSFFHPK,OK
slimfinder,15120800001,35,Q.[ST][IL]..F,0.001,DPOD3_HUMAN__Q15054,456,462,466,QVSITGF,Q.[ST][IL]..F,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,QVSITGF,OK
slimfinder,15120800001,35,Q.[ST][IL]..F,0.001,MSH3_YEAST__P25336,4,10,1018,QPTISRF,Q.[ST][IL]..F,0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,QPTISRF,OK
slimfinder,15120800001,35,Q.[ST][IL]..F,0.001,DPOD3_SCHPO__P30261,362,368,372,QKSIMSF,Q.[ST][IL]..F,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSF,OK
slimfinder,15120800001,35,Q.[ST][IL]..F,0.001,RRM3_YEAST__P38766,35,41,723,QQTLSSF,Q.[ST][IL]..F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSF,OK
slimfinder,15120800001,35,Q.[ST][IL]..F,0.001,UNG_HUMAN__P13051,4,10,313,QKTLYSF,Q.[ST][IL]..F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSF,OK
slimfinder,15120800001,35,Q.[ST][IL]..F,0.001,DNLI1_YEAST__P04819,38,44,755,QATLARF,Q.[ST][IL]..F,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,QATLARF,OK
slimfinder,15120800001,35,Q.[ST][IL]..F,0.001,DPOD3_YEAST__P47110,338,344,350,QGTLESF,Q.[ST][IL]..F,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESF,OK
slimfinder,15120800001,35,Q.[ST][IL]..F,0.001,MSH6_HUMAN__P52701,4,10,1360,QSTLYSF,Q.[ST][IL]..F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSF,OK
slimfinder,15120800001,35,Q.[ST][IL]..F,0.001,UNG_YEAST__P12887,21,27,359,QTTIEDF,Q.[ST][IL]..F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,QTTIEDF,OK
slimfinder,15120800001,35,Q.[ST][IL]..F,0.001,DNLI1_HUMAN__P18858,2,8,919,QRSIMSF,Q.[ST][IL]..F,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSF,OK
slimfinder,15120800001,36,[KR]Q.TL..F,0.002,DNLI1_YEAST__P04819,37,44,755,KQATLARF,[KR]Q.TL..F,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,KQATLARF,OK
slimfinder,15120800001,36,[KR]Q.TL..F,0.002,DPOD3_YEAST__P47110,337,344,350,KQGTLESF,[KR]Q.TL..F,0,RecName: Full=DNA polymerase delta subunit 3;,KQGTLESF,OK
slimfinder,15120800001,36,[KR]Q.TL..F,0.002,RRM3_YEAST__P38766,34,41,723,RQQTLSSF,[KR]Q.TL..F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,RQQTLSSF,OK
slimfinder,15120800001,36,[KR]Q.TL..F,0.002,MSH6_HUMAN__P52701,3,10,1360,RQSTLYSF,[KR]Q.TL..F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,RQSTLYSF,OK
slimfinder,15120800001,37,"Q.T.{1,2}S.{0,1}FF",0.002,MSH3_YEAST__P25336,4,11,1018,QPTISRFF,Q.T.S.FF,0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,QPTISRFF,OK
slimfinder,15120800001,37,"Q.T.{1,2}S.{0,1}FF",0.002,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q.T..SFF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,37,"Q.T.{1,2}S.{0,1}FF",0.002,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q.T..SFF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,37,"Q.T.{1,2}S.{0,1}FF",0.002,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q.T..SFF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,37,"Q.T.{1,2}S.{0,1}FF",0.002,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q.T..SFF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,DNLI1_YEAST__P04819,41,45,755,LARFF,[ILM]..F[FY],0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,LARFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,DPOD3_HUMAN__Q15054,459,463,466,ITGFF,[ILM]..F[FY],0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,ITGFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,MSH3_YEAST__P25336,7,11,1018,ISRFF,[ILM]..F[FY],0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,ISRFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,FEN1_HUMAN__P39748,340,344,380,LDDFF,[ILM]..F[FY],0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;,LDDFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,FEN1_HUMAN__P39748,65,69,380,MGMFY,[ILM]..F[FY],0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;,MGMFY,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,DPOD3_SCHPO__P30261,365,369,372,IMSFF,[ILM]..F[FY],0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,IMSFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,ERCC5_HUMAN__P28715,993,997,1186,IDSFF,[ILM]..F[FY],0,RecName: Full=DNA repair protein complementing XP-G cells; EC=3.1.-.-; AltName: Full=DNA excision repair protein ERCC-5; AltName: Full=Xeroderma pigmentosum group G-complementing protein;,IDSFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,UNG_YEAST__P12887,24,28,359,IEDFF,[ILM]..F[FY],0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,IEDFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,UNG_HUMAN__P13051,7,11,313,LYSFF,[ILM]..F[FY],0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,LYSFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,RFC1_YEAST__P38630,4,8,861,ISDFF,[ILM]..F[FY],0,RecName: Full=Replication factor C subunit 1; Short=Replication factor C1; AltName: Full=Activator 1 95 kDa subunit; AltName: Full=Cell division control protein 44;,ISDFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,RRM3_YEAST__P38766,38,42,723,LSSFF,[ILM]..F[FY],0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,LSSFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,DPOD3_YEAST__P47110,341,345,350,LESFF,[ILM]..F[FY],0,RecName: Full=DNA polymerase delta subunit 3;,LESFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,MSH6_HUMAN__P52701,7,11,1360,LYSFF,[ILM]..F[FY],0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,LYSFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,MSH6_YEAST__Q03834,30,34,1242,LLSFF,[ILM]..F[FY],0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,LLSFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,CDN1A_HUMAN__P38936,147,151,164,MTDFY,[ILM]..F[FY],0,RecName: Full=Cyclin-dependent kinase inhibitor 1; AltName: Full=CDK-interacting protein 1; AltName: Full=Melanoma differentiation-associated protein 6; Short=MDA-6; AltName: Full=p21;,MTDFY,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,FEN1_YEAST__P26793,343,347,382,LDGFF,[ILM]..F[FY],0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;,LDGFF,Warning: DG
slimfinder,15120800001,38,[ILM]..F[FY],0.004,FEN1_YEAST__P26793,66,70,382,MGMFY,[ILM]..F[FY],0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;,MGMFY,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,RAD2_YEAST__P07276,998,1002,1031,INEFF,[ILM]..F[FY],0,RecName: Full=DNA repair protein RAD2; EC=3.1.-.-;,INEFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,DNLI1_HUMAN__P18858,5,9,919,IMSFF,[ILM]..F[FY],0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,IMSFF,OK
slimfinder,15120800001,38,[ILM]..F[FY],0.004,DNLI1_HUMAN__P18858,228,232,919,LSSFF,[ILM]..F[FY],0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,LSSFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,DNLI1_YEAST__P04819,41,45,755,LARFF,[IL]..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,LARFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,DPOD3_HUMAN__Q15054,459,463,466,ITGFF,[IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,ITGFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,MSH3_YEAST__P25336,7,11,1018,ISRFF,[IL]..FF,0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,ISRFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,FEN1_HUMAN__P39748,340,344,380,LDDFF,[IL]..FF,0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;,LDDFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,DPOD3_SCHPO__P30261,365,369,372,IMSFF,[IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,IMSFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,ERCC5_HUMAN__P28715,993,997,1186,IDSFF,[IL]..FF,0,RecName: Full=DNA repair protein complementing XP-G cells; EC=3.1.-.-; AltName: Full=DNA excision repair protein ERCC-5; AltName: Full=Xeroderma pigmentosum group G-complementing protein;,IDSFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,UNG_HUMAN__P13051,7,11,313,LYSFF,[IL]..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,LYSFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,RFC1_YEAST__P38630,4,8,861,ISDFF,[IL]..FF,0,RecName: Full=Replication factor C subunit 1; Short=Replication factor C1; AltName: Full=Activator 1 95 kDa subunit; AltName: Full=Cell division control protein 44;,ISDFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,RRM3_YEAST__P38766,38,42,723,LSSFF,[IL]..FF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,LSSFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,DPOD3_YEAST__P47110,341,345,350,LESFF,[IL]..FF,0,RecName: Full=DNA polymerase delta subunit 3;,LESFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,MSH6_HUMAN__P52701,7,11,1360,LYSFF,[IL]..FF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,LYSFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,MSH6_YEAST__Q03834,30,34,1242,LLSFF,[IL]..FF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,LLSFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,UNG_YEAST__P12887,24,28,359,IEDFF,[IL]..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,IEDFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,FEN1_YEAST__P26793,343,347,382,LDGFF,[IL]..FF,0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;,LDGFF,Warning: DG
slimfinder,15120800001,39,[IL]..FF,0.006,RAD2_YEAST__P07276,998,1002,1031,INEFF,[IL]..FF,0,RecName: Full=DNA repair protein RAD2; EC=3.1.-.-;,INEFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,DNLI1_HUMAN__P18858,5,9,919,IMSFF,[IL]..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,IMSFF,OK
slimfinder,15120800001,39,[IL]..FF,0.006,DNLI1_HUMAN__P18858,228,232,919,LSSFF,[IL]..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,LSSFF,OK
slimfinder,15120800001,40,TL.S.F,0.010,DNLI1_HUMAN__P18858,227,232,919,TLSSFF,TL.S.F,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,TLSSFF,OK
slimfinder,15120800001,40,TL.S.F,0.010,DPOD3_YEAST__P47110,340,345,350,TLESFF,TL.S.F,0,RecName: Full=DNA polymerase delta subunit 3;,TLESFF,OK
slimfinder,15120800001,40,TL.S.F,0.010,RRM3_YEAST__P38766,37,42,723,TLSSFF,TL.S.F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,TLSSFF,OK
slimfinder,15120800001,40,TL.S.F,0.010,MSH6_HUMAN__P52701,6,11,1360,TLYSFF,TL.S.F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,TLYSFF,OK
slimfinder,15120800001,40,TL.S.F,0.010,UNG_HUMAN__P13051,6,11,313,TLYSFF,TL.S.F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,TLYSFF,OK
slimfinder,15120800001,41,TL.SF,0.011,DNLI1_HUMAN__P18858,227,231,919,TLSSF,TL.SF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,TLSSF,OK
slimfinder,15120800001,41,TL.SF,0.011,DPOD3_YEAST__P47110,340,344,350,TLESF,TL.SF,0,RecName: Full=DNA polymerase delta subunit 3;,TLESF,OK
slimfinder,15120800001,41,TL.SF,0.011,RRM3_YEAST__P38766,37,41,723,TLSSF,TL.SF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,TLSSF,OK
slimfinder,15120800001,41,TL.SF,0.011,MSH6_HUMAN__P52701,6,10,1360,TLYSF,TL.SF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,TLYSF,OK
slimfinder,15120800001,41,TL.SF,0.011,UNG_HUMAN__P13051,6,10,313,TLYSF,TL.SF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,TLYSF,OK
slimfinder,15120800001,42,I..FF..K,0.011,DNLI1_HUMAN__P18858,5,12,919,IMSFFHPK,I..FF..K,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,IMSFFHPK,OK
slimfinder,15120800001,42,I..FF..K,0.011,DPOD3_HUMAN__Q15054,459,466,466,ITGFFQRK,I..FF..K,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,ITGFFQRK,OK
slimfinder,15120800001,42,I..FF..K,0.011,UNG_YEAST__P12887,24,31,359,IEDFFGTK,I..FF..K,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,IEDFFGTK,OK
slimfinder,15120800001,42,I..FF..K,0.011,DPOD3_SCHPO__P30261,365,372,372,IMSFFGKK,I..FF..K,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,IMSFFGKK,OK
slimfinder,15120800001,43,Q.SI..FF,0.013,DNLI1_HUMAN__P18858,2,9,919,QRSIMSFF,Q.SI..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,QRSIMSFF,OK
slimfinder,15120800001,43,Q.SI..FF,0.013,DPOD3_HUMAN__Q15054,456,463,466,QVSITGFF,Q.SI..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,QVSITGFF,OK
slimfinder,15120800001,43,Q.SI..FF,0.013,DPOD3_SCHPO__P30261,362,369,372,QKSIMSFF,Q.SI..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,QKSIMSFF,OK
slimfinder,15120800001,44,"Q.T.{1,2}S.F",0.019,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q.T..S.F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,44,"Q.T.{1,2}S.F",0.019,MSH3_YEAST__P25336,4,10,1018,QPTISRF,Q.T.S.F,0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,QPTISRF,OK
slimfinder,15120800001,44,"Q.T.{1,2}S.F",0.019,RRM3_YEAST__P38766,35,41,723,QQTLSSF,Q.T.S.F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSF,OK
slimfinder,15120800001,44,"Q.T.{1,2}S.F",0.019,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q.T..S.F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,44,"Q.T.{1,2}S.F",0.019,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q.T..S.F,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,44,"Q.T.{1,2}S.F",0.019,DNMT1_HUMAN__P26358,164,171,1616,QTTITSHF,Q.T..S.F,0,RecName: Full=DNA (cytosine-5)-methyltransferase 1; Short=Dnmt1; EC=2.1.1.37; AltName: Full=CXXC-type zinc finger protein 9; AltName: Full=DNA methyltransferase HsaI; Short=DNA MTase HsaI; Short=M.HsaI; AltName: Full=MCMT;,QTTITSHF,OK
slimfinder,15120800001,44,"Q.T.{1,2}S.F",0.019,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q.T..S.F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,45,"Q.T..S.{0,1}F",0.020,DPOD3_YEAST__P47110,338,344,350,QGTLESF,Q.T..SF,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESF,OK
slimfinder,15120800001,45,"Q.T..S.{0,1}F",0.020,DPOD3_YEAST__P47110,338,345,350,QGTLESFF,Q.T..S.F,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESFF,OK
slimfinder,15120800001,45,"Q.T..S.{0,1}F",0.020,MSH6_HUMAN__P52701,4,10,1360,QSTLYSF,Q.T..SF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSF,OK
slimfinder,15120800001,45,"Q.T..S.{0,1}F",0.020,MSH6_HUMAN__P52701,4,11,1360,QSTLYSFF,Q.T..S.F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSFF,OK
slimfinder,15120800001,45,"Q.T..S.{0,1}F",0.020,RRM3_YEAST__P38766,35,41,723,QQTLSSF,Q.T..SF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSF,OK
slimfinder,15120800001,45,"Q.T..S.{0,1}F",0.020,RRM3_YEAST__P38766,35,42,723,QQTLSSFF,Q.T..S.F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSFF,OK
slimfinder,15120800001,45,"Q.T..S.{0,1}F",0.020,UNG_HUMAN__P13051,4,10,313,QKTLYSF,Q.T..SF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSF,OK
slimfinder,15120800001,45,"Q.T..S.{0,1}F",0.020,UNG_HUMAN__P13051,4,11,313,QKTLYSFF,Q.T..S.F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSFF,OK
slimfinder,15120800001,45,"Q.T..S.{0,1}F",0.020,DNMT1_HUMAN__P26358,164,171,1616,QTTITSHF,Q.T..S.F,0,RecName: Full=DNA (cytosine-5)-methyltransferase 1; Short=Dnmt1; EC=2.1.1.37; AltName: Full=CXXC-type zinc finger protein 9; AltName: Full=DNA methyltransferase HsaI; Short=DNA MTase HsaI; Short=M.HsaI; AltName: Full=MCMT;,QTTITSHF,OK
slimfinder,15120800001,46,L..FF,0.026,FEN1_YEAST__P26793,343,347,382,LDGFF,L..FF,0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;,LDGFF,Warning: DG
slimfinder,15120800001,46,L..FF,0.026,FEN1_HUMAN__P39748,340,344,380,LDDFF,L..FF,0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;,LDDFF,OK
slimfinder,15120800001,46,L..FF,0.026,RRM3_YEAST__P38766,38,42,723,LSSFF,L..FF,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,LSSFF,OK
slimfinder,15120800001,46,L..FF,0.026,UNG_HUMAN__P13051,7,11,313,LYSFF,L..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,LYSFF,OK
slimfinder,15120800001,46,L..FF,0.026,DNLI1_YEAST__P04819,41,45,755,LARFF,L..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,LARFF,OK
slimfinder,15120800001,46,L..FF,0.026,DPOD3_YEAST__P47110,341,345,350,LESFF,L..FF,0,RecName: Full=DNA polymerase delta subunit 3;,LESFF,OK
slimfinder,15120800001,46,L..FF,0.026,MSH6_HUMAN__P52701,7,11,1360,LYSFF,L..FF,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,LYSFF,OK
slimfinder,15120800001,46,L..FF,0.026,MSH6_YEAST__Q03834,30,34,1242,LLSFF,L..FF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,LLSFF,OK
slimfinder,15120800001,46,L..FF,0.026,DNLI1_HUMAN__P18858,228,232,919,LSSFF,L..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,LSSFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,DNLI1_YEAST__P04819,41,45,755,LARFF,[ILMV]..F[FY],0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,LARFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,DPOD3_HUMAN__Q15054,459,463,466,ITGFF,[ILMV]..F[FY],0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,ITGFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,MSH3_YEAST__P25336,7,11,1018,ISRFF,[ILMV]..F[FY],0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,ISRFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,FEN1_HUMAN__P39748,340,344,380,LDDFF,[ILMV]..F[FY],0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;,LDDFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,FEN1_HUMAN__P39748,65,69,380,MGMFY,[ILMV]..F[FY],0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;,MGMFY,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,DPOD3_SCHPO__P30261,365,369,372,IMSFF,[ILMV]..F[FY],0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,IMSFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,ERCC5_HUMAN__P28715,993,997,1186,IDSFF,[ILMV]..F[FY],0,RecName: Full=DNA repair protein complementing XP-G cells; EC=3.1.-.-; AltName: Full=DNA excision repair protein ERCC-5; AltName: Full=Xeroderma pigmentosum group G-complementing protein;,IDSFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,UNG_YEAST__P12887,24,28,359,IEDFF,[ILMV]..F[FY],0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,IEDFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,UNG_HUMAN__P13051,7,11,313,LYSFF,[ILMV]..F[FY],0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,LYSFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,RFC1_YEAST__P38630,4,8,861,ISDFF,[ILMV]..F[FY],0,RecName: Full=Replication factor C subunit 1; Short=Replication factor C1; AltName: Full=Activator 1 95 kDa subunit; AltName: Full=Cell division control protein 44;,ISDFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,RRM3_YEAST__P38766,38,42,723,LSSFF,[ILMV]..F[FY],0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,LSSFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,RRM3_YEAST__P38766,712,716,723,VKDFY,[ILMV]..F[FY],0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,VKDFY,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,DPOD3_YEAST__P47110,341,345,350,LESFF,[ILMV]..F[FY],0,RecName: Full=DNA polymerase delta subunit 3;,LESFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,DNMT1_HUMAN__P26358,1018,1022,1616,VNKFY,[ILMV]..F[FY],0,RecName: Full=DNA (cytosine-5)-methyltransferase 1; Short=Dnmt1; EC=2.1.1.37; AltName: Full=CXXC-type zinc finger protein 9; AltName: Full=DNA methyltransferase HsaI; Short=DNA MTase HsaI; Short=M.HsaI; AltName: Full=MCMT;,VNKFY,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,CDN1A_HUMAN__P38936,147,151,164,MTDFY,[ILMV]..F[FY],0,RecName: Full=Cyclin-dependent kinase inhibitor 1; AltName: Full=CDK-interacting protein 1; AltName: Full=Melanoma differentiation-associated protein 6; Short=MDA-6; AltName: Full=p21;,MTDFY,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,MSH6_YEAST__Q03834,30,34,1242,LLSFF,[ILMV]..F[FY],0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,LLSFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,MSH6_HUMAN__P52701,7,11,1360,LYSFF,[ILMV]..F[FY],0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,LYSFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,FEN1_YEAST__P26793,343,347,382,LDGFF,[ILMV]..F[FY],0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;,LDGFF,Warning: DG
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,FEN1_YEAST__P26793,66,70,382,MGMFY,[ILMV]..F[FY],0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;,MGMFY,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,RAD2_YEAST__P07276,998,1002,1031,INEFF,[ILMV]..F[FY],0,RecName: Full=DNA repair protein RAD2; EC=3.1.-.-;,INEFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,DNLI1_HUMAN__P18858,5,9,919,IMSFF,[ILMV]..F[FY],0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,IMSFF,OK
slimfinder,15120800001,47,[ILMV]..F[FY],0.037,DNLI1_HUMAN__P18858,228,232,919,LSSFF,[ILMV]..F[FY],0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,LSSFF,OK
slimfinder,15120800001,48,I..FF,0.048,DPOD3_HUMAN__Q15054,459,463,466,ITGFF,I..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;,ITGFF,OK
slimfinder,15120800001,48,I..FF,0.048,MSH3_YEAST__P25336,7,11,1018,ISRFF,I..FF,0,RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;,ISRFF,OK
slimfinder,15120800001,48,I..FF,0.048,DPOD3_SCHPO__P30261,365,369,372,IMSFF,I..FF,0,RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;,IMSFF,OK
slimfinder,15120800001,48,I..FF,0.048,ERCC5_HUMAN__P28715,993,997,1186,IDSFF,I..FF,0,RecName: Full=DNA repair protein complementing XP-G cells; EC=3.1.-.-; AltName: Full=DNA excision repair protein ERCC-5; AltName: Full=Xeroderma pigmentosum group G-complementing protein;,IDSFF,OK
slimfinder,15120800001,48,I..FF,0.048,RFC1_YEAST__P38630,4,8,861,ISDFF,I..FF,0,RecName: Full=Replication factor C subunit 1; Short=Replication factor C1; AltName: Full=Activator 1 95 kDa subunit; AltName: Full=Cell division control protein 44;,ISDFF,OK
slimfinder,15120800001,48,I..FF,0.048,UNG_YEAST__P12887,24,28,359,IEDFF,I..FF,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;,IEDFF,OK
slimfinder,15120800001,48,I..FF,0.048,RAD2_YEAST__P07276,998,1002,1031,INEFF,I..FF,0,RecName: Full=DNA repair protein RAD2; EC=3.1.-.-;,INEFF,OK
slimfinder,15120800001,48,I..FF,0.048,DNLI1_HUMAN__P18858,5,9,919,IMSFF,I..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;,IMSFF,OK
slimfinder,15120800001,49,KQ..L..FF,0.093,DNLI1_YEAST__P04819,37,45,755,KQATLARFF,KQ..L..FF,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,KQATLARFF,OK
slimfinder,15120800001,49,KQ..L..FF,0.093,DPOD3_YEAST__P47110,337,345,350,KQGTLESFF,KQ..L..FF,0,RecName: Full=DNA polymerase delta subunit 3;,KQGTLESFF,OK
slimfinder,15120800001,49,KQ..L..FF,0.093,MSH6_YEAST__Q03834,26,34,1242,KQSSLLSFF,KQ..L..FF,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,KQSSLLSFF,OK
slimfinder,15120800001,50,Q..L..F,0.098,DNLI1_YEAST__P04819,38,44,755,QATLARF,Q..L..F,0,RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;,QATLARF,OK
slimfinder,15120800001,50,Q..L..F,0.098,FEN1_YEAST__P26793,340,346,382,QGRLDGF,Q..L..F,0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;,QGRLDGF,Warning: DG
slimfinder,15120800001,50,Q..L..F,0.098,FEN1_HUMAN__P39748,337,343,380,QGRLDDF,Q..L..F,0,RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;,QGRLDDF,OK
slimfinder,15120800001,50,Q..L..F,0.098,RRM3_YEAST__P38766,35,41,723,QQTLSSF,Q..L..F,0,RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};,QQTLSSF,OK
slimfinder,15120800001,50,Q..L..F,0.098,UNG_HUMAN__P13051,4,10,313,QKTLYSF,Q..L..F,0,RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};,QKTLYSF,OK
slimfinder,15120800001,50,Q..L..F,0.098,DPOD3_YEAST__P47110,338,344,350,QGTLESF,Q..L..F,0,RecName: Full=DNA polymerase delta subunit 3;,QGTLESF,OK
slimfinder,15120800001,50,Q..L..F,0.098,MSH6_HUMAN__P52701,4,10,1360,QSTLYSF,Q..L..F,0,RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;,QSTLYSF,OK
slimfinder,15120800001,50,Q..L..F,0.098,MSH6_YEAST__Q03834,27,33,1242,QSSLLSF,Q..L..F,0,RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;,QSSLLSF,OK
#slimfinder# 18 Seq; 8 UPC; 15.196 MST; blaste=1.00e-04, blastcf=F, blastf=T
UP	N	MST	Seqs
1	1	1.000	CDN1A_HUMAN__P38936
2	3	2.537	DNLI1_HUMAN__P18858 DNLI1_YEAST__P04819 DNMT1_HUMAN__P26358
3	4	3.369	DPOD3_HUMAN__Q15054 MSH3_YEAST__P25336 MSH6_YEAST__Q03834 MSH6_HUMAN__P52701
4	5	3.722	DPOD3_SCHPO__P30261 FEN1_HUMAN__P39748 ERCC5_HUMAN__P28715 FEN1_YEAST__P26793 RAD2_YEAST__P07276
5	1	1.000	DPOD3_YEAST__P47110
6	1	1.000	RFC1_YEAST__P38630
7	1	1.000	RRM3_YEAST__P38766
8	2	1.569	UNG_HUMAN__P13051 UNG_YEAST__P12887
slimfinder: 18 Seq, 8 UPC, 50 Sig SLiMs in 1 Clouds

Cloud 1 (50 SLiMs):	Q..[IL].SFF	Q.[ST]..SFF	Q.[ST][IL]..FF	Q.TL..FF	Q..L..FF	[ST][IL].SFF	TL.SFF	Q.[ST][IL].S.F	Q.[ST][IL].SF	Q..[IL]..FF	Q..I..FF..K	Q.T..SFF	[IL].SFF	TL.{0,1}S.{0,1}FF	Q..L.SFF	Q..I..FF.{1,2}K	TL..FF	Q..[IL].S.F	Q..[IL].SF	K..Q..[IL]..FF	[ST]..SFF	[KR]Q..L..FF	Q.TL..F	Q.TL.S.F	T..SFF	Q.TL.SF	[ST][IL]..FF	Q..I..FF	Q.[ST]..S.F	[KR]..TL..FF	Q.[ST]..SF	L.SFF	Q.T..S.F	I..FF.{1,2}K	Q.[ST][IL]..F	[KR]Q.TL..F	[ILM]..F[FY]	[IL]..FF	TL.S.F	TL.SF	I..FF..K	Q.SI..FF	Q.T..S.{0,1}F	L..FF	[ILMV]..F[FY]	I..FF	KQ..L..FF	Q..L..F	Q.T.{1,2}S.{0,1}FF	Q.T.{1,2}S.F	(p = 3.42e-12)
8 UPC	18 Seq:	CDN1A_HUMAN__P38936	DNLI1_HUMAN__P18858	DNLI1_YEAST__P04819	DNMT1_HUMAN__P26358	DPOD3_HUMAN__Q15054	DPOD3_SCHPO__P30261	DPOD3_YEAST__P47110	ERCC5_HUMAN__P28715	FEN1_HUMAN__P39748	FEN1_YEAST__P26793	MSH3_YEAST__P25336	MSH6_HUMAN__P52701	MSH6_YEAST__Q03834	RAD2_YEAST__P07276	RFC1_YEAST__P38630	RRM3_YEAST__P38766	UNG_HUMAN__P13051	UNG_YEAST__P12887

SLiMMaker Consensus: [RST][ILM]..F[FY]
- SLiM matches 17 of 23 sequences (73.9%).

LKKQGTLESFFKRK
MSRQSTLYSFFPKS
AYRQQTLSSFFMGC
MIGQKTLYSFFSPS
STRQTTITSHFAKG
RRAPKTLSSFFTPR
--MQRSIMSFFHPK
KPQQKSIMSFFGKK
KMKQSSLLSFFSKQ
KPKQATLARFFTSM
MAGQPTISRFFKKA
ANRQVSITGFFQRK
KRKQTTIEDFFGTK
KGKQKRINEFFPRE
GSTQGRLDDFFKVT
SGIQGRLDGFFQVV
QQTQLRIDSFFRLA
---MVNISDFFGKN
KRRQTSMTDFYHSK
ETTSHLMGMFYRTI
ETTSHLMGMFYRTL
TDIKIRVNKFYRPE
IRTNERVKDFYKRL


#Cloud Seq coverage/overlap
Cloud	Dataset	1
1:Q..[IL].SFF	1.000	1.000


#Cloud UPC coverage/overlap
Cloud	Dataset	1
1:Q..[IL].SFF	1.000	1.000

>CDN1A_HUMAN__P38936 RecName: Full=Cyclin-dependent kinase inhibitor 1; AltName: Full=CDK-interacting protein 1; AltName: Full=Melanoma differentiation-associated protein 6; Short=MDA-6; AltName: Full=p21;
XSEPAGDVRQNPCGSKACRRLFGPXXXXQLSXXCXAXXXXXXXXXXXXWXXDFVTXXXXXXDFAWERXXGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP
>DNLI1_HUMAN__P18858 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAALKEWNGVVSESDSPVKRPGRKAARVLGSEGXXXDEALSPAKGQKPALDCSQVSPPRPATSPENNASLSDTSPMDSSPSGIPKRRTARKQLPKRTIQEVLEEQSEDEDREAKRKKEXXXXXTPKESLTEAEVATEKEGEDGDQPTTPPKPLKTSKAETPTESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPLDPSGYNPAKNNYHPVEDACWKPGQKXXXXXVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQQGLELGVGDXXXXKXVAQAXXRQLESVRAEAAEKGDVGLVAENSRSTQRLMLPPPPLTASGVFSKFXDIARLXGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLSQAVSLTPPGQEFPPAMVDAGKGKTAEARKTWLEEQGXILXXTFXXXXXXXXXXXXXXXXXXXXLXEHCKLSPGIPLKPMLAHPTRGISEVLKRXXXXXXXXEXXYXXXRAQIHALEGGEVKIFSRNQEDNTGKYPDIISRIPXXXXXXXXXXXXXXEXXXWXXXXXXXXPFQVLXTRXRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSXXXXXLREXXXXXXXXFVXATSLDXXXXEQIAEFLEQXVXXXXXXLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLXXYXXXXXXLQAICKLGTGFSDEELEEHHQSLKALVLPSPXXXXXXXGAVXXXXXXXXXXXXXXXXXXXXXXXXXXXAXGXVXXDKXXXXXFPRFIRVREDKQPEQATTSAQVACLYRKQSXIXNXQGEDSGSDPEDTY
>DNLI1_YEAST__P04819 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;
XRRLLTGCLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNVSGEEEYATKKLKQTAVTHTVAAPSSMGSNFSSIPSSAPSSGVADSPQQSQRLVGEVEDALSSNNNDHYSSNIPYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXISETXXXSMSQIKLKYXXXXXXXXIAMGARNVQPTMFKPKPLTVGEVFKNLRAIAKTQGKDSQLKKMKLIXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLHDENREDSPDKDVPMDVLESAQQKIRDXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPXXXMLAKPTKAINEVLDRFQGETFTSEYKYDGERAQVHLLNDGTMRIYSRNGENMTERYPEINITDFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLTXXTKXXXXXFQYATQITTXXLDELQKFLDESVNHSCEGLMVKMLEGPESHYEPSKRSRNWLKLKKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXCKXXXXXXXXXLQLXHDRLTPTIXXGPKATFVFXSSAEXXXXXEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFLRXREDKGVEDATSSDQIVELYENQSHMQN
>DNMT1_HUMAN__P26358 RecName: Full=DNA (cytosine-5)-methyltransferase 1; Short=Dnmt1; EC=2.1.1.37; AltName: Full=CXXC-type zinc finger protein 9; AltName: Full=DNA methyltransferase HsaI; Short=DNA MTase HsaI; Short=M.HsaI; AltName: Full=MCMT;
XPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKXXVXXXXNXXXXXXXXXXXXXXXXXXXXLRXXXLSEEXYLAKVXSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKXXXRDXKXEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSAKPIYDDDPSLEGGVNGKNLGPINEWWITXFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTYEDLINKIETTVPPSGLNLNRFTEDXXLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRXXXKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRSKQACQERRCPNMAMKEADXXEEVXDNIPEMPSPKKMHQGKXXXQNKNRISWVGEAVKTDXXXXXXXXXXXXXXXXXXXXCVSVXXXXXXXXXXXAXXXXXXXXXXXXXXXXAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPXXNWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCXXXXXXXXXXQXXIXRVLEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFXXXIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXCVQXYXXXXXXXXXFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTXDVFSGCGGXXEGFHQXGXXDTXXAIXXXXXXXQAFRLNNPGSXXXXXXXXXXXXLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPEXXXXXXXXXXXXXXXXXXXXXXXXXTRLXXXPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAXXQPILRDXXXXXXXXLXXXRMRXXXXAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXAXXXXXXXXXGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILXKHRQVGNAVPPPLXXXXXXXXXXXXXXXXXXSASAKIKEEEAAKD
>DPOD3_HUMAN__Q15054 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;
XXDQLYLEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXDYVERKRKENSGAQLHVTYLVSXSLIXXXXSCHKVAVVREXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXXXXXQCAAAVPRAPAESXXXSKKFEQSHLHMSSETQANNELTTNGHGPPASKQVSQQPKGIMGMFASKAAAKTQETNKETKTEAKEVTNASAAGNKAPGKGNMMSNFFGKAAMNKFKVNLDSEQAVKEEKIVEQPTVSVTEPKLATPAGLKKSSKKAEPVKVLQKEKKRGKRVALSDDETKETENMRKKRRRIKLPESDSSEDEVFPDSPGAYEAESPSXXXXXSXXLEPVPKTEPEPPSVKSSSGENKRKRKRVLKSKTYLDGEGCIVTEKVYESESCTDSEEELNMKTSSVHRPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK
>DPOD3_YEAST__P47110 RecName: Full=DNA polymerase delta subunit 3;
XDQKASYFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSXXXXXSESSKIIERTKTLEEKSKPLVRPTARSKTTPEETTGRKSKSKDMGLRSTALLAKMKKDRDDKETSRQNELRKRKEENLQKINKQNPEREAQMKELNNLFVEDDLDTEEVNGGSKPNSPKETDSNDKDKNNDDLEDLLETTAEDSLMDVPKIQQTKPSETEHSKEPKSEEEPSSFIDEDGYIVTKRPATSTPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK
>DPOD3_SCHPO__P30261 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;
XEEWRNFLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLXXXXXXDXEINLEIDEESQPIXNFPVLXXXXCDKXXLQXKQSRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVXXXXXXXXXXXFIFNENSVPRVLKKAPSTHSPQLSVPSKTSTIDKTDTRSTEKTKGKDIFSNARNQKGNSSRKNKKAPLENHKEKEPLLPKEEKLSEQAKRERDDLKNIMQLEDESVSTTSVHDSEDDNLDSNNFQLEIGTEAKSAAPDEPQEIIKSVSGGKRRGKRKVKKYATTKDEEGFLVTKEEEVWESFSEDENISTGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK
>ERCC5_HUMAN__P28715 RecName: Full=DNA repair protein complementing XP-G cells; EC=3.1.-.-; AltName: Full=DNA excision repair protein ERCC-5; AltName: Full=Xeroderma pigmentosum group G-complementing protein;
XGVQGLWKLXXXXXXXXXXXAXXXXXXXXXXXXXXXXXXXXXXDRHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQTLVKRRQRKDLASSDSRKTTEKLLKTFLKRQAIKTAFRSKRDEALPSLTQVRRENDLYVLPPLQEEEKHSSEXXDXKEWQERMNQKQALQEEFFHNPQAIDIESEDFSSLPPEVKHEILTDMKEFTKRRRTLFEAMPEESDDFSQYQLKGLLKKNYLNQHIEHVQKEMNQQHSGHIRRQYEDEGGFLKEVESRRVVSEDTSHYILIKGIQAKXVAEVDSEXLPXXSKMHGMSFDVKSSPCEKLKTEKEPDATPPSPRTLLAMQAALLGSSSEXXLXSENRRQARGRNAPAAVDEGSISPRTLSAIKRALDDDEDVKVCAGDDVQTGGPGAEEMRINSSTENSDEGLKVRDGKGIPFTATLASSSVNSAEEHVASTNEGREPTDSVPKEQMSLVHVGTEAFPISDESMIKDRKDRLPLESAVVRHSDAPGLPNGRELTPASPTCTNSVSKNETHAEVLEQQNELCPYESKFDSSLLSSDDETKCKPNSASEVIGPVSLQETSSIVSVPSEAVDNVENVVSFNAKEHENFLETIQEQQTTESAGQDLISIPKAVEPMEIDSEESESDGSFIEVQSVISDEELQAEFPETSKPPSEQGEEELVGTREGEAPAESESLLRDNSERDDVDGEPQEAEKDAEDSLHEWQDINLEELETLESNLLAQQNSLKAQKQQQERIAATVTGXXXXXXXXXXXXXXXXXXXXXXXXXXXCAILDLTDQTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGXXXLLKFSEWWHEAQKNPKIRPNPHDTKVKKKLRTLQLTPGFPNPAVAEAYLKPVXXXSKXSFLWGKXDXXXXXXXXXXXFGXXXXXXXXXLFPVLKQXXXXXTXXRIDSFFRLAXQEKEDAKRIKSQRLNRAVTCMLRKEKEAAASEIEAVSXAMEKEFELLDKAKGKTQKRGITNTLEESSSLKRKRLSDSKGKNTCGGFLGETCLSEXXDGXXSEDAESSSLMNVQRRTAAKEPKTSASDSQNSVKEAPVKNGGATTSXXXDSDDDGGKEKMVLVTARSVFGKKRXKLXXAXGXKRKT
>FEN1_HUMAN__P39748 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;
XGIQGLAKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXDVLQNEEGETTSHLMGMFYRTIXXXXXXIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNXXXKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLXASXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRAVDLIXKHXXXEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK
>FEN1_YEAST__P26793 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;
XGIKGLNAIXXXXXXXXXXXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXDGGQLTNEAGETTSHLMGMFYXXLXXXXXXXKPCYVFDGKPPDLKSHELTKRSSRRVETEKKLAEATTELEKMKQERRLVKVSKEHNEEAQKLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXKEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVEFIESXESNNTKWKIPEDWPYKQARMLFLDPEVXXGNEINLKWSPPKEKELIEYLCDDKKXSEERVKSGISRLKKGLKSGIQXRLDGFFQVVPKTKEQLAXXXKRAQENKKLNKNKNKVTKGRR
>MSH3_YEAST__P25336 RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;
XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLDTDEEDNLSSVASTTVTNDSFPLKGSVSSKNSKNSEKTSGTSTTFNDIDFAKKLDRIMKRRSDENVEAXDDXXXGXEDFVKKKARKSPTAKLTPLDKQVKDLKMHHRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIDESNPQXXXXRQXXXXXXXXXXXXXXXXXXXXXXXKVAXXEQAETSAIKKHDPGASKSSVFERKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRXXXXXXXXXXXXXXXXXXXXXXXXDEFEEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRIXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLSXXFKSSDGRIGXXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQXMDFFNXXXXXXXXGIIKIQRESESXRSQLKXXXXXXXXXXXXXXXXXXXXXXXXXXXXNXXXXXLPDDWIKXNNTKMVSRFTTPRTQKLTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSLXXXYVPNDIMMXPENGKINIITGPNMXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXDYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSLDIH
>MSH6_HUMAN__P52701 RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;
XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGASPSPGGDAAWSEAGPGPRPLARSASPPKAKNLNGGLRRSVAPAAPTSCDFSPGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXKXXXXXXHVQFXXXSPXRGWVSKRLLKPYTGSKSKEAQKGGHFYSAKPEILRAMQRADEALNKDKIKRLELAVCDEPSXPXXXXXMEVGTTYVTDKSEEDNEIXSXXEVQPKTQGSRRSSRQIKKRRVISDSESDIGGSDVEFKPDTKEEGSSDEISSGVGDSESEGLNSPVKVARKRKRMVTGNGSLKRKSSRKETPSATKQATSISSETKNTLRAFSAPQNSESQAHVSGGGDDSSRPTVWYHETLEWLKEEKRXDEHXXRPDHPDFDASTLYVPEDFLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRXXXXXXXXGYKVARVEQTETPEMMEARCRKMAHISKXXRXXXXXICXIXXXGTQTYSVLEGDPSENYSKYLLSLKEKEEDSSGHTRAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFEKGNLXKXTKTILKSSXSCSLXXGLIXGXQFWXXXKTXXXXXEEEXXXXXXSDGXXVMLPQVLKGMTSESDSIGLTPGEKSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSDXXXXXXXGAXXXXXXXXXXXXXXXXXXXXXFLNGXNGXTEXTLLERVDXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLSKIHNVGSPLKSQNHPDSRAIMYEETXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVISLQTKNPEGRFPDLTVELNRWDTAFDHEKARKTGLITPKAGFDSDYDQALADIRXXEQSLLEYLEKXXXXXXXXXXXXXXXXXXXXXXXIPENFTXRNLPEEYELKSTKKGCKRYWTKXXXXXXXNLIXXEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXCRPVILLXXXXPPFLELKGSRHPXXXXTFFXXXXXPNDILIGCEEEXXXXXKAYCVLVTXXXXXGKXTLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGAXXXXXXXXSXFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXENXCXXXXXXXXXXXXXXXXXXXXXXXXXXAXXLXXXPEEVIQKGHRKAREFEKMNXXXXXXREXXXXXXXXXXXXXXXXXXXXLIKEL
>MSH6_YEAST__Q03834 RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;
XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKITKNPQGGKTGKLFVDVDEDNDLTIAEETVSTVRSDIMHSQEPQSDTMLNSNTTEPKSTTTDEDLSSSQSRRNHKRRVNYAESDXXXSDTTFTAKRKKGKVVDSESDEDEYLPDKNDGXEXXXIAXDKEDIKGELAEDSGXXXDLISLAETTSKKKFSYNTSHSSSPFTRNISRDNSKKKSRPNQAPSRSYNPSHSQPSATSKSSKFNKQNEERYQWLVDERDAQRRPKSDPEYDPRTLYIPXSAWXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQRESMLAKEMREGSKGIVKRELQCILXXGTLXXXXXXXXXXXXXXXXXXXXXXXFYNETQLDXXXXVXXXXXXXXXXXXXXXXXXELQMLEFEDDSECTKLDTLMSQVRPMEVVMERNNLXXXXNKIXXXXXXXXXXXXXVKXGXXXXXXXKTXXXXISSEYFXTEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLFNRAITXXXXRMMKKWLXHPLXXXXXIEXXXXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXDVSKXXXXXXXXXXXXVKSWXXXFEXXKAINENIIVPQRGFDIEFDKSMDRIQELEXXXXXXXXXXXXXXXXXNIXYXXXXXXXXXXEIPIXXXXXXPSNXVQMXXXKXXXXXXSDEVXXLXXSMAEAKEIHKTXEEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXAPSCRPTIVDEVDSKTXXQLNGFLKFXXXXXXXFNXGATTAXXFIPNDIELGKEQPRXXLLTGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGANDXXXXXXXXFXXXXXXXXXXXXXXXXXXXXXVDELGXXXXSSDGFAXXEXXXXXXXXXXXXXXXXXXXXXXXXXSFKHHPXXRPLKMSILXXXXXXXXXXLYKXXXXXXXXXFXMHVAXXXXXXXXXIXXAQIAADNLEHTSRLVKERDLAANNLNGEVVSVPGXXXXXXXXIAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIDDLQS
>RAD2_YEAST__P07276 RecName: Full=DNA repair protein RAD2; EC=3.1.-.-;
XGVHSFWDIAXPXXXXVRLESLEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRETIRQRKERRQGKRESAKSTARKLLALQLQNGSNDNVKNSTPXXGXSVQIFKPQDEWDLPDIPGFKYDKEDARVNSNKTFEKLMNSINGDGLEDIDLDTINPASAEFEEXPKXXXXXXXXXXXXXXXXXMXXXXEQLXTIXXXSXXXXXXXIXXXXXXXXFXQKLINTTGFQDGGASKLNEEVINRISGQKSKEYKLTKTNNGWILGLGANDXXDAQKAIVIDDKDAGALVKQLDSNAEDGDVLRWDDLEDNSLKIVRHESSNATTAPQKRSNRSEDEGCDSDECXWXXVELKPKNVKFVEDFSXKAARLPYMGQSLNNAGSKSFLDKRHDQASPSKTTPTMRISRISVEDDDEDYLKQIEEIEMMEAVQLSKMEKKPEADDKSKIAKPVTSKGTEARPPIVQYGLLGAQPDSKQPYHVTNLNSKSESVIKRTSKTVLSEFRPPSQQEDKGAILTEGEQNLNFISHKIPQFDFNNENSLLFQKNTESNVSQEATKEKSPIPEMPSWFSSTASQQLYNPYNTTNFVEDKNVRNEQESGAETTNKGSSYELLTGLNATEILERESEKESSNDENKDDDLEVLSEELFEDVPTKSQISKEAEDNDSRKVESINKEHRKPLIFDYDFSEDEEDNIVENMIKEQEEFDTFKNTTLSTSAERNVAENAFVEDELFEQQMKDKRDSDEVTMDMIKEXQXXXXXXXXXXXXXPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGXXXMXXXXXXXVXXEXXXXXNXKDWYNNGQFDKRKQETENKFEKDLRKKLVXNEIXXXXXXXXXXXXDAYMRPXXXXDTTPFVWXXXXXXXXXXFMKTQLGWPHEKSDEILIPLIRDVNKRXXXGXQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM
>RFC1_YEAST__P38630 RecName: Full=Replication factor C subunit 1; Short=Replication factor C1; AltName: Full=Activator 1 95 kDa subunit; AltName: Full=Cell division control protein 44;
XVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLDTESDQESTNKTPKKMPVSNVIDVSETPEGEKKLPLPAKRKASSPTVKPASSKKTKPSXKXXDXASNITAQDVLDKIPSLDLSNVHVKENAKFDFKSANSNADPDEIVSEIGSFPEGKPXXXXXXXXXXXXXXXXXXXXAXXALAKRYGARVTXSXXXKTSVVVLGDEAGPKXLEKIKQLKIKAIDEEGFKQLIAGMPAEGGDGEAAEKARRKLEEQHNIATKEAELLVKKEEERSKKLAATRVSGGHLERDNVVREEDKLWTVKYAPTNLQQVCGNKGSVMKLKNWLANWENSKKNSFKHAGKDGSGVFRAAMLYGPPGIXKTTAAHXXXXXXXXXXXEQNXXDVRSKTLLNAGXKXXXXXXXVVGYFKHNEEAQXXNGKHFVIIMDEVDGMSGXDRXXVGQLAQFCXXXXXXXXXXCNERNXXXXXXXXXXXLDIXXXRXXXXSXKSRLMXXXXXXXXXXXXXXIDXXIXXXXXXXXXXINLLXXXSTXXKXINHENINEIXXAWXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQXXXXSTRPSVLKPGQSHLXXXAEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGFTRKYNSMTHPVAIYRTGSTIXXXXVGTSTSTPDFEDVVDADDNPVPADDEETQDSSTDLKKDKLIKQKAKPTKRKTATSKPGGSKKRKTKA
>RRM3_YEAST__P38766 RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};
XFRSHASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRNITAPPRPRLIRNNSXXLFXQSQGSFGDDDPDAEFKKLVDVPRLNSYKKSSRSLSMTSSLHKTASASTTQKTYHFDEDETLREVTSVKSNSRQLSFTSTINIEDSSMKLSTDSERPAKRSKPSMEFQGLKLTVPKKIKPLLRKTVSNMDSMNHRSASSPVVLTMEQERVVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIRKXXXXXGXXQXXLXXXXXXXXXXAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXAPXXLYATRREVEXXNVKKLXXXXXXXYEFKAVDXXXXXXXXILXXXXXXXXXXXXXXXXQXXXXXNKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXEXXEFRQXLNARXXXXXXXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXXXXXXXXXXXXXPRENXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXDXGKXXXNERVKDFYKRLETLK
>UNG_HUMAN__P13051 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESGDAAAIPAKKAPAGQEEPGTPPSSPLSAEQLDRIQRNKAAALLRLXXXXXXXXXXEXXXKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPXXXXXXXXQXXXXXXXXXXILGQDPYHGPNQAHGLCFSVQRPVXXXPSLENIYKELSTDIEDFVHPGHGDLSXWAKXXXXXXXXXXXXXAHQANSHKERGWEXFTDAVVXXXXXXXXXXXXXXXXXXXXXXGSAIDRKRHHVLQTAHPSPXXVYRGFFGXXXXSKTNELLQKSGKKPIDWKEL
>UNG_YEAST__P12887 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;
XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTETKAVAKEANTDKYPANSNAKDVYSKNLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFXXXXQADHTVFPPAXXXXXXXXXXXXXXXXXXXXGXDPXHXFNQAHGLAFSVKPXTXAXPSLKNIYKELKQEYPDFVEDNKVGDLXXWASXXXXXXNXSLTVRAHNANSHSKHGWETXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSXGSXXKYPNIMVMKSVHPXXLSASRGFFGXXXXXXXXXWXXXXXXXKMIDWSVVPGTSLREVQEANARLESESKDP
>CDN1A_HUMAN__P38936-slimfinder Motifs
--------------------------------------------------------------------------------------------------------------------------------------------------M--FY-------------
>CDN1A_HUMAN__P38936-masked
XSEPAGDVRQNPCGSKACRRLFGPXXXXQLSXXCXAXXXXXXXXXXXXWXXDFVTXXXXXXDFAWERXXGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP
>CDN1A_HUMAN__P38936 RecName: Full=Cyclin-dependent kinase inhibitor 1; AltName: Full=CDK-interacting protein 1; AltName: Full=Melanoma differentiation-associated protein 6; Short=MDA-6; AltName: Full=p21;
MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP
>DNLI1_HUMAN__P18858-slimfinder Motifs
-Q-SI-SFF--K----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------TL-SFF---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>DNLI1_HUMAN__P18858-masked
XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAALKEWNGVVSESDSPVKRPGRKAARVLGSEGXXXDEALSPAKGQKPALDCSQVSPPRPATSPENNASLSDTSPMDSSPSGIPKRRTARKQLPKRTIQEVLEEQSEDEDREAKRKKEXXXXXTPKESLTEAEVATEKEGEDGDQPTTPPKPLKTSKAETPTESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPLDPSGYNPAKNNYHPVEDACWKPGQKXXXXXVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQQGLELGVGDXXXXKXVAQAXXRQLESVRAEAAEKGDVGLVAENSRSTQRLMLPPPPLTASGVFSKFXDIARLXGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLSQAVSLTPPGQEFPPAMVDAGKGKTAEARKTWLEEQGXILXXTFXXXXXXXXXXXXXXXXXXXXLXEHCKLSPGIPLKPMLAHPTRGISEVLKRXXXXXXXXEXXYXXXRAQIHALEGGEVKIFSRNQEDNTGKYPDIISRIPXXXXXXXXXXXXXXEXXXWXXXXXXXXPFQVLXTRXRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSXXXXXLREXXXXXXXXFVXATSLDXXXXEQIAEFLEQXVXXXXXXLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLXXYXXXXXXLQAICKLGTGFSDEELEEHHQSLKALVLPSPXXXXXXXGAVXXXXXXXXXXXXXXXXXXXXXXXXXXXAXGXVXXDKXXXXXFPRFIRVREDKQPEQATTSAQVACLYRKQSXIXNXQGEDSGSDPEDTY
>DNLI1_HUMAN__P18858 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKEWNGVVSESDSPVKRPGRKAARVLGSEGEEEDEALSPAKGQKPALDCSQVSPPRPATSPENNASLSDTSPMDSSPSGIPKRRTARKQLPKRTIQEVLEEQSEDEDREAKRKKEEEEEETPKESLTEAEVATEKEGEDGDQPTTPPKPLKTSKAETPTESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPLDPSGYNPAKNNYHPVEDACWKPGQKVPYLAVARTFEKIEEVSARLRMVETLSNLLRSVVALSPPDLLPVLYLSLNHLGPPQQGLELGVGDGVLLKAVAQATGRQLESVRAEAAEKGDVGLVAENSRSTQRLMLPPPPLTASGVFSKFRDIARLTGSASTAKKIDIIKGLFVACRHSEARFIARSLSGRLRLGLAEQSVLAALSQAVSLTPPGQEFPPAMVDAGKGKTAEARKTWLEEQGMILKQTFCEVPDLDRIIPVLLEHGLERLPEHCKLSPGIPLKPMLAHPTRGISEVLKRFEEAAFTCEYKYDGQRAQIHALEGGEVKIFSRNQEDNTGKYPDIISRIPKIKLPSVTSFILDTEAVAWDREKKQIQPFQVLTTRKRKEVDASEIQVQVCLYAFDLIYLNGESLVREPLSRRRQLLRENFVETEGEFVFATSLDTKDIEQIAEFLEQSVKDSCEGLMVKTLDVDATYEIAKRSHNWLKLKKDYLDGVGDTLDLVVIGAYLGRGKRAGRYGGFLLASYDEDSEELQAICKLGTGFSDEELEEHHQSLKALVLPSPRPYVRIDGAVIPDHWLDPSAVWEVKCADLSLSPIYPAARGLVDSDKGISLRFPRFIRVREDKQPEQATTSAQVACLYRKQSQIQNQQGEDSGSDPEDTY
>DNLI1_YEAST__P04819-slimfinder Motifs
----------------------------------K-KQ-TL--FF--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>DNLI1_YEAST__P04819-masked
XRRLLTGCLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNVSGEEEYATKKLKQTAVTHTVAAPSSMGSNFSSIPSSAPSSGVADSPQQSQRLVGEVEDALSSNNNDHYSSNIPYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXISETXXXSMSQIKLKYXXXXXXXXIAMGARNVQPTMFKPKPLTVGEVFKNLRAIAKTQGKDSQLKKMKLIXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLHDENREDSPDKDVPMDVLESAQQKIRDXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPXXXMLAKPTKAINEVLDRFQGETFTSEYKYDGERAQVHLLNDGTMRIYSRNGENMTERYPEINITDFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLTXXTKXXXXXFQYATQITTXXLDELQKFLDESVNHSCEGLMVKMLEGPESHYEPSKRSRNWLKLKKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXCKXXXXXXXXXLQLXHDRLTPTIXXGPKATFVFXSSAEXXXXXEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFLRXREDKGVEDATSSDQIVELYENQSHMQN
>DNLI1_YEAST__P04819 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;
MRRLLTGCLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNVSGEEEYATKKLKQTAVTHTVAAPSSMGSNFSSIPSSAPSSGVADSPQQSQRLVGEVEDALSSNNNDHYSSNIPYSEVCEVFNKIEAISSRLEIIRICSDFFIKIMKQSSKNLIPTTYLFINRLGPDYEAGLELGLGENLLMKTISETCGKSMSQIKLKYKDIGDLGEIAMGARNVQPTMFKPKPLTVGEVFKNLRAIAKTQGKDSQLKKMKLIKRMLTACKGIEAKFLIRSLESKLRIGLAEKTVLISLSKALLLHDENREDSPDKDVPMDVLESAQQKIRDAFCQVPNYEIVINSCLEHGIMNLDKYCTLRPGIPLKPMLAKPTKAINEVLDRFQGETFTSEYKYDGERAQVHLLNDGTMRIYSRNGENMTERYPEINITDFIQDLDTTKNLILDCEAVAWDKDQGKILPFQVLSTRKRKDVELNDVKVKVCLFAFDILCYNDERLINKSLKERREYLTKVTKVVPGEFQYATQITTNNLDELQKFLDESVNHSCEGLMVKMLEGPESHYEPSKRSRNWLKLKKDYLEGVGDSLDLCVLGAYYGRGKRTGTYGGFLLGCYNQDTGEFETCCKIGTGFSDEMLQLLHDRLTPTIIDGPKATFVFDSSAEPDVWFEPTTLFEVLTADLSLSPIYKAGSATFDKGVSLRFPRFLRIREDKGVEDATSSDQIVELYENQSHMQN
>DNMT1_HUMAN__P26358-slimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------Q-TI-S-F------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------V--FY------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>DNMT1_HUMAN__P26358-masked
XPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKXXVXXXXNXXXXXXXXXXXXXXXXXXXXLRXXXLSEEXYLAKVXSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKXXXRDXKXEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSAKPIYDDDPSLEGGVNGKNLGPINEWWITXFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTYEDLINKIETTVPPSGLNLNRFTEDXXLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRXXXKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRSKQACQERRCPNMAMKEADXXEEVXDNIPEMPSPKKMHQGKXXXQNKNRISWVGEAVKTDXXXXXXXXXXXXXXXXXXXXCVSVXXXXXXXXXXXAXXXXXXXXXXXXXXXXAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPXXNWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCXXXXXXXXXXQXXIXRVLEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFXXXIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXCVQXYXXXXXXXXXFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTXDVFSGCGGXXEGFHQXGXXDTXXAIXXXXXXXQAFRLNNPGSXXXXXXXXXXXXLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPEXXXXXXXXXXXXXXXXXXXXXXXXXTRLXXXPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAXXQPILRDXXXXXXXXLXXXRMRXXXXAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXAXXXXXXXXXGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILXKHRQVGNAVPPPLXXXXXXXXXXXXXXXXXXSASAKIKEEEAAKD
>DNMT1_HUMAN__P26358 RecName: Full=DNA (cytosine-5)-methyltransferase 1; Short=Dnmt1; EC=2.1.1.37; AltName: Full=CXXC-type zinc finger protein 9; AltName: Full=DNA methyltransferase HsaI; Short=DNA MTase HsaI; Short=M.HsaI; AltName: Full=MCMT;
MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQLCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEKEEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGLNLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQQPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQGKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLAEMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD
>DPOD3_HUMAN__Q15054-slimfinder Motifs
-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------Q-SI--FF--K
>DPOD3_HUMAN__Q15054-masked
XXDQLYLEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXDYVERKRKENSGAQLHVTYLVSXSLIXXXXSCHKVAVVREXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXXXXXQCAAAVPRAPAESXXXSKKFEQSHLHMSSETQANNELTTNGHGPPASKQVSQQPKGIMGMFASKAAAKTQETNKETKTEAKEVTNASAAGNKAPGKGNMMSNFFGKAAMNKFKVNLDSEQAVKEEKIVEQPTVSVTEPKLATPAGLKKSSKKAEPVKVLQKEKKRGKRVALSDDETKETENMRKKRRRIKLPESDSSEDEVFPDSPGAYEAESPSXXXXXSXXLEPVPKTEPEPPSVKSSSGENKRKRKRVLKSKTYLDGEGCIVTEKVYESESCTDSEEELNMKTSSVHRPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK
>DPOD3_HUMAN__Q15054 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;
MADQLYLENIDEFVTDQNKIVTYKWLSYTLGVHVNQAKQMLYDYVERKRKENSGAQLHVTYLVSGSLIQNGHSCHKVAVVREDKLEAVKSKLAVTASIHVYSIQKAMLKDSGPLFNTDYDILKSNLQNCSKFSAIQCAAAVPRAPAESSSSSKKFEQSHLHMSSETQANNELTTNGHGPPASKQVSQQPKGIMGMFASKAAAKTQETNKETKTEAKEVTNASAAGNKAPGKGNMMSNFFGKAAMNKFKVNLDSEQAVKEEKIVEQPTVSVTEPKLATPAGLKKSSKKAEPVKVLQKEKKRGKRVALSDDETKETENMRKKRRRIKLPESDSSEDEVFPDSPGAYEAESPSPPPPPSPPLEPVPKTEPEPPSVKSSSGENKRKRKRVLKSKTYLDGEGCIVTEKVYESESCTDSEEELNMKTSSVHRPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK
>DPOD3_YEAST__P47110-slimfinder Motifs
------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------KQ-TL-SFF-----
>DPOD3_YEAST__P47110-masked
XDQKASYFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSXXXXXSESSKIIERTKTLEEKSKPLVRPTARSKTTPEETTGRKSKSKDMGLRSTALLAKMKKDRDDKETSRQNELRKRKEENLQKINKQNPEREAQMKELNNLFVEDDLDTEEVNGGSKPNSPKETDSNDKDKNNDDLEDLLETTAEDSLMDVPKIQQTKPSETEHSKEPKSEEEPSSFIDEDGYIVTKRPATSTPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK
>DPOD3_YEAST__P47110 RecName: Full=DNA polymerase delta subunit 3;
MDQKASYFINEKLFTEVKPVLFTDLIHHLKIGPSMAKKLMFDYYKQTTNAKYNCVVICCYKDQTIKIIHDLSNIPQQDSIIDCFIYAFNPMDSFIPYYDIIDQKDCLTIKNSYELKVSESSKIIERTKTLEEKSKPLVRPTARSKTTPEETTGRKSKSKDMGLRSTALLAKMKKDRDDKETSRQNELRKRKEENLQKINKQNPEREAQMKELNNLFVEDDLDTEEVNGGSKPNSPKETDSNDKDKNNDDLEDLLETTAEDSLMDVPKIQQTKPSETEHSKEPKSEEEPSSFIDEDGYIVTKRPATSTPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK
>DPOD3_SCHPO__P30261-slimfinder Motifs
----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------K--Q-SI-SFF-KK
>DPOD3_SCHPO__P30261-masked
XEEWRNFLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLXXXXXXDXEINLEIDEESQPIXNFPVLXXXXCDKXXLQXKQSRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVXXXXXXXXXXXFIFNENSVPRVLKKAPSTHSPQLSVPSKTSTIDKTDTRSTEKTKGKDIFSNARNQKGNSSRKNKKAPLENHKEKEPLLPKEEKLSEQAKRERDDLKNIMQLEDESVSTTSVHDSEDDNLDSNNFQLEIGTEAKSAAPDEPQEIIKSVSGGKRRGKRKVKKYATTKDEEGFLVTKEEEVWESFSEDENISTGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK
>DPOD3_SCHPO__P30261 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;
MEEWRNFLDIKVINESSLVTVDNLSLQLDISSEKAQEYLNMFYQGNDFLYPIYLIHGQPIDDEINLEIDEESQPISNFPVLQYILCDKSSLQEKQSRLKSGYKTVIFALSSAPLSDFDELLPAVYEIREKDVLYKKEDADKYGFIFNENSVPRVLKKAPSTHSPQLSVPSKTSTIDKTDTRSTEKTKGKDIFSNARNQKGNSSRKNKKAPLENHKEKEPLLPKEEKLSEQAKRERDDLKNIMQLEDESVSTTSVHDSEDDNLDSNNFQLEIGTEAKSAAPDEPQEIIKSVSGGKRRGKRKVKKYATTKDEEGFLVTKEEEVWESFSEDENISTGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK
>ERCC5_HUMAN__P28715-slimfinder Motifs
--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------I-SFF---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>ERCC5_HUMAN__P28715-masked
XGVQGLWKLXXXXXXXXXXXAXXXXXXXXXXXXXXXXXXXXXXDRHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQTLVKRRQRKDLASSDSRKTTEKLLKTFLKRQAIKTAFRSKRDEALPSLTQVRRENDLYVLPPLQEEEKHSSEXXDXKEWQERMNQKQALQEEFFHNPQAIDIESEDFSSLPPEVKHEILTDMKEFTKRRRTLFEAMPEESDDFSQYQLKGLLKKNYLNQHIEHVQKEMNQQHSGHIRRQYEDEGGFLKEVESRRVVSEDTSHYILIKGIQAKXVAEVDSEXLPXXSKMHGMSFDVKSSPCEKLKTEKEPDATPPSPRTLLAMQAALLGSSSEXXLXSENRRQARGRNAPAAVDEGSISPRTLSAIKRALDDDEDVKVCAGDDVQTGGPGAEEMRINSSTENSDEGLKVRDGKGIPFTATLASSSVNSAEEHVASTNEGREPTDSVPKEQMSLVHVGTEAFPISDESMIKDRKDRLPLESAVVRHSDAPGLPNGRELTPASPTCTNSVSKNETHAEVLEQQNELCPYESKFDSSLLSSDDETKCKPNSASEVIGPVSLQETSSIVSVPSEAVDNVENVVSFNAKEHENFLETIQEQQTTESAGQDLISIPKAVEPMEIDSEESESDGSFIEVQSVISDEELQAEFPETSKPPSEQGEEELVGTREGEAPAESESLLRDNSERDDVDGEPQEAEKDAEDSLHEWQDINLEELETLESNLLAQQNSLKAQKQQQERIAATVTGXXXXXXXXXXXXXXXXXXXXXXXXXXXCAILDLTDQTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGXXXLLKFSEWWHEAQKNPKIRPNPHDTKVKKKLRTLQLTPGFPNPAVAEAYLKPVXXXSKXSFLWGKXDXXXXXXXXXXXFGXXXXXXXXXLFPVLKQXXXXXTXXRIDSFFRLAXQEKEDAKRIKSQRLNRAVTCMLRKEKEAAASEIEAVSXAMEKEFELLDKAKGKTQKRGITNTLEESSSLKRKRLSDSKGKNTCGGFLGETCLSEXXDGXXSEDAESSSLMNVQRRTAAKEPKTSASDSQNSVKEAPVKNGGATTSXXXDSDDDGGKEKMVLVTARSVFGKKRXKLXXAXGXKRKT
>ERCC5_HUMAN__P28715 RecName: Full=DNA repair protein complementing XP-G cells; EC=3.1.-.-; AltName: Full=DNA excision repair protein ERCC-5; AltName: Full=Xeroderma pigmentosum group G-complementing protein;
MGVQGLWKLLECSGRQVSPEALEGKILAVDISIWLNQALKGVRDRHGNSIENPHLLTLFHRLCKLLFFRIRPIFVFDGDAPLLKKQTLVKRRQRKDLASSDSRKTTEKLLKTFLKRQAIKTAFRSKRDEALPSLTQVRRENDLYVLPPLQEEEKHSSEEEDEKEWQERMNQKQALQEEFFHNPQAIDIESEDFSSLPPEVKHEILTDMKEFTKRRRTLFEAMPEESDDFSQYQLKGLLKKNYLNQHIEHVQKEMNQQHSGHIRRQYEDEGGFLKEVESRRVVSEDTSHYILIKGIQAKTVAEVDSESLPSSSKMHGMSFDVKSSPCEKLKTEKEPDATPPSPRTLLAMQAALLGSSSEEELESENRRQARGRNAPAAVDEGSISPRTLSAIKRALDDDEDVKVCAGDDVQTGGPGAEEMRINSSTENSDEGLKVRDGKGIPFTATLASSSVNSAEEHVASTNEGREPTDSVPKEQMSLVHVGTEAFPISDESMIKDRKDRLPLESAVVRHSDAPGLPNGRELTPASPTCTNSVSKNETHAEVLEQQNELCPYESKFDSSLLSSDDETKCKPNSASEVIGPVSLQETSSIVSVPSEAVDNVENVVSFNAKEHENFLETIQEQQTTESAGQDLISIPKAVEPMEIDSEESESDGSFIEVQSVISDEELQAEFPETSKPPSEQGEEELVGTREGEAPAESESLLRDNSERDDVDGEPQEAEKDAEDSLHEWQDINLEELETLESNLLAQQNSLKAQKQQQERIAATVTGQMFLESQELLRLFGIPYIQAPMEAEAQCAILDLTDQTSGTITDDSDIWLFGARHVYRNFFNKNKFVEYYQYVDFHNQLGLDRNKLINLAYLLGSDYTEGIPTVGCVTAMEILNEFPGHGLEPLLKFSEWWHEAQKNPKIRPNPHDTKVKKKLRTLQLTPGFPNPAVAEAYLKPVVDDSKGSFLWGKPDLDKIREFCQRYFGWNRTKTDESLFPVLKQLDAQQTQLRIDSFFRLAQQEKEDAKRIKSQRLNRAVTCMLRKEKEAAASEIEAVSVAMEKEFELLDKAKGKTQKRGITNTLEESSSLKRKRLSDSKGKNTCGGFLGETCLSESSDGSSSEDAESSSLMNVQRRTAAKEPKTSASDSQNSVKEAPVKNGGATTSSSSDSDDDGGKEKMVLVTARSVFGKKRRKLRRARGRKRKT
>FEN1_HUMAN__P39748-slimfinder Motifs
----------------------------------------------------------------M--FY---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------Q--L--FF------------------------------------
>FEN1_HUMAN__P39748-masked
XGIQGLAKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXDVLQNEEGETTSHLMGMFYRTIXXXXXXIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNXXXKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLXASXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRAVDLIXKHXXXEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK
>FEN1_HUMAN__P39748 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;
MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK
>FEN1_YEAST__P26793-slimfinder Motifs
-----------------------------------------------------------------M--FY-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------Q--L--FF-----------------------------------
>FEN1_YEAST__P26793-masked
XGIKGLNAIXXXXXXXXXXXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXDGGQLTNEAGETTSHLMGMFYXXLXXXXXXXKPCYVFDGKPPDLKSHELTKRSSRRVETEKKLAEATTELEKMKQERRLVKVSKEHNEEAQKLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXKEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVEFIESXESNNTKWKIPEDWPYKQARMLFLDPEVXXGNEINLKWSPPKEKELIEYLCDDKKXSEERVKSGISRLKKGLKSGIQXRLDGFFQVVPKTKEQLAXXXKRAQENKKLNKNKNKVTKGRR
>FEN1_YEAST__P26793 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;
MGIKGLNAIISEHVPSAIRKSDIKSFFGRKVAIDASMSLYQFLIAVRQQDGGQLTNEAGETTSHLMGMFYRTLRMIDNGIKPCYVFDGKPPDLKSHELTKRSSRRVETEKKLAEATTELEKMKQERRLVKVSKEHNEEAQKLLGLMGIPYIIAPTEAEAQCAELAKKGKVYAAASEDMDTLCYRTPFLLRHLTFSEAKKEPIHEIDTELVLRGLDLTIEQFVDLCIMLGCDYCESIRGVGPVTALKLIKTHGSIEKIVEFIESGESNNTKWKIPEDWPYKQARMLFLDPEVIDGNEINLKWSPPKEKELIEYLCDDKKFSEERVKSGISRLKKGLKSGIQGRLDGFFQVVPKTKEQLAAAAKRAQENKKLNKNKNKVTKGRR
>MSH3_YEAST__P25336-slimfinder Motifs
---Q-TIS-FF-K---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>MSH3_YEAST__P25336-masked
XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLDTDEEDNLSSVASTTVTNDSFPLKGSVSSKNSKNSEKTSGTSTTFNDIDFAKKLDRIMKRRSDENVEAXDDXXXGXEDFVKKKARKSPTAKLTPLDKQVKDLKMHHRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIDESNPQXXXXRQXXXXXXXXXXXXXXXXXXXXXXXKVAXXEQAETSAIKKHDPGASKSSVFERKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRXXXXXXXXXXXXXXXXXXXXXXXXDEFEEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRIXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLSXXFKSSDGRIGXXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQXMDFFNXXXXXXXXGIIKIQRESESXRSQLKXXXXXXXXXXXXXXXXXXXXXXXXXXXXNXXXXXLPDDWIKXNNTKMVSRFTTPRTQKLTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSLXXXYVPNDIMMXPENGKINIITGPNMXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXDYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSLDIH
>MSH3_YEAST__P25336 RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;
MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLDTDEEDNLSSVASTTVTNDSFPLKGSVSSKNSKNSEKTSGTSTTFNDIDFAKKLDRIMKRRSDENVEAEDDEEEGEEDFVKKKARKSPTAKLTPLDKQVKDLKMHHRDKVLVIRVGYKYKCFAEDAVTVSRILHIKLVPGKLTIDESNPQDCNHRQFAYCSFPDVRLNVHLERLVHHNLKVAVVEQAETSAIKKHDPGASKSSVFERKISNVFTKATFGVNSTFVLRGKRILGDTNSIWALSRDVHQGKVAKYSLISVNLNNGEVVYDEFEEPNLADEKLQIRIKYLQPIEVLVNTDDLPLHVAKFFKDISCPLIHKQEYDLEDHVVQAIKVMNEKIQLSPSLIRLVSKLYSHMVEYNNEQVMLIPSIYSPFASKIHMLLDPNSLQSLDIFTHDGGKGSLFWLLDHTRTSFGLRMLREWILKPLVDVHQIEERLDAIECITSEINNSIFFESLNQMLNHTPDLLRTLNRIMYGTTSRKEVYFYLKQITSFVDHFKMHQSYLSEHFKSSDGRIGKQSPLLFRLFSELNELLSTTQLPHFLTMINVSAVMEKNSDKQVMDFFNLNNYDCSEGIIKIQRESESVRSQLKEELAEIRKYLKRPYLNFRDEVDYLIEVKNSQIKDLPDDWIKVNNTKMVSRFTTPRTQKLTQKLEYYKDLLIRESELQYKEFLNKITAEYTELRKITLNLAQYDCILSLAATSCNVNYVRPTFVNGQQAIIAKNARNPIIESLDVHYVPNDIMMSPENGKINIITGPNMGGKSSYIRQVALLTIMAQIGSFVPAEEIRLSIFENVLTRIGAHDDIINGDSTFKVEMLDILHILKNCNKRSLLLLDEVGRGTGTHDGIAISYALIKYFSELSDCPLILFTTHFPMLGEIKSPLIRNYHMDYVEEQKTGEDWMSVIFLYKLKKGLTYNSYGMNVAKLARLDKDIINRAFSISEELRKESINEDALKLFSSLKRILKSDNITATDKLAKLLSLDIH
>MSH6_HUMAN__P52701-slimfinder Motifs
--RQ-TL-SFF-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>MSH6_HUMAN__P52701-masked
XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGASPSPGGDAAWSEAGPGPRPLARSASPPKAKNLNGGLRRSVAPAAPTSCDFSPGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXKXXXXXXHVQFXXXSPXRGWVSKRLLKPYTGSKSKEAQKGGHFYSAKPEILRAMQRADEALNKDKIKRLELAVCDEPSXPXXXXXMEVGTTYVTDKSEEDNEIXSXXEVQPKTQGSRRSSRQIKKRRVISDSESDIGGSDVEFKPDTKEEGSSDEISSGVGDSESEGLNSPVKVARKRKRMVTGNGSLKRKSSRKETPSATKQATSISSETKNTLRAFSAPQNSESQAHVSGGGDDSSRPTVWYHETLEWLKEEKRXDEHXXRPDHPDFDASTLYVPEDFLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRXXXXXXXXGYKVARVEQTETPEMMEARCRKMAHISKXXRXXXXXICXIXXXGTQTYSVLEGDPSENYSKYLLSLKEKEEDSSGHTRAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFEKGNLXKXTKTILKSSXSCSLXXGLIXGXQFWXXXKTXXXXXEEEXXXXXXSDGXXVMLPQVLKGMTSESDSIGLTPGEKSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSDXXXXXXXGAXXXXXXXXXXXXXXXXXXXXXFLNGXNGXTEXTLLERVDXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLSKIHNVGSPLKSQNHPDSRAIMYEETXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVISLQTKNPEGRFPDLTVELNRWDTAFDHEKARKTGLITPKAGFDSDYDQALADIRXXEQSLLEYLEKXXXXXXXXXXXXXXXXXXXXXXXIPENFTXRNLPEEYELKSTKKGCKRYWTKXXXXXXXNLIXXEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXCRPVILLXXXXPPFLELKGSRHPXXXXTFFXXXXXPNDILIGCEEEXXXXXKAYCVLVTXXXXXGKXTLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGAXXXXXXXXSXFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXENXCXXXXXXXXXXXXXXXXXXXXXXXXXXAXXLXXXPEEVIQKGHRKAREFEKMNXXXXXXREXXXXXXXXXXXXXXXXXXXXLIKEL
>MSH6_HUMAN__P52701 RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;
MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGASPSPGGDAAWSEAGPGPRPLARSASPPKAKNLNGGLRRSVAPAAPTSCDFSPGDLVWAKMEGYPWWPCLVYNHPFDGTFIREKGKSVRVHVQFFDDSPTRGWVSKRLLKPYTGSKSKEAQKGGHFYSAKPEILRAMQRADEALNKDKIKRLELAVCDEPSEPEEEEEMEVGTTYVTDKSEEDNEIESEEEVQPKTQGSRRSSRQIKKRRVISDSESDIGGSDVEFKPDTKEEGSSDEISSGVGDSESEGLNSPVKVARKRKRMVTGNGSLKRKSSRKETPSATKQATSISSETKNTLRAFSAPQNSESQAHVSGGGDDSSRPTVWYHETLEWLKEEKRRDEHRRRPDHPDFDASTLYVPEDFLNSCTPGMRKWWQIKSQNFDLVICYKVGKFYELYHMDALIGVSELGLVFMKGNWAHSGFPEIAFGRYSDSLVQKGYKVARVEQTETPEMMEARCRKMAHISKYDRVVRREICRIITKGTQTYSVLEGDPSENYSKYLLSLKEKEEDSSGHTRAYGVCFVDTSLGKFFIGQFSDDRHCSRFRTLVAHYPPVQVLFEKGNLSKETKTILKSSLSCSLQEGLIPGSQFWDASKTLRTLLEEEYFREKLSDGIGVMLPQVLKGMTSESDSIGLTPGEKSELALSALGGCVFYLKKCLIDQELLSMANFEEYIPLDSDTVSTTRSGAIFTKAYQRMVLDAVTLNNLEIFLNGTNGSTEGTLLERVDTCHTPFGKRLLKQWLCAPLCNHYAINDRLDAIEDLMVVPDKISEVVELLKKLPDLERLLSKIHNVGSPLKSQNHPDSRAIMYEETTYSKKKIIDFLSALEGFKVMCKIIGIMEEVADGFKSKILKQVISLQTKNPEGRFPDLTVELNRWDTAFDHEKARKTGLITPKAGFDSDYDQALADIRENEQSLLEYLEKQRNRIGCRTIVYWGIGRNRYQLEIPENFTTRNLPEEYELKSTKKGCKRYWTKTIEKKLANLINAEERRDVSLKDCMRRLFYNFDKNYKDWQSAVECIAVLDVLLCLANYSRGGDGPMCRPVILLPEDTPPFLELKGSRHPCITKTFFGDDFIPNDILIGCEEEEQENGKAYCVLVTGPNMGGKSTLMRQAGLLAVMAQMGCYVPAEVCRLTPIDRVFTRLGASDRIMSGESTFFVELSETASILMHATAHSLVLVDELGRGTATFDGTAIANAVVKELAETIKCRTLFSTHYHSLVEDYSQNVAVRLGHMACMVENECEDPSQETITFLYKFIKGACPKSYGFNAARLANLPEEVIQKGHRKAREFEKMNQSLRLFREVCLASERSTVDAEAVHKLLTLIKEL
>MSH6_YEAST__Q03834-slimfinder Motifs
-----------------------K-KQ-SL-SFF--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>MSH6_YEAST__Q03834-masked
XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKITKNPQGGKTGKLFVDVDEDNDLTIAEETVSTVRSDIMHSQEPQSDTMLNSNTTEPKSTTTDEDLSSSQSRRNHKRRVNYAESDXXXSDTTFTAKRKKGKVVDSESDEDEYLPDKNDGXEXXXIAXDKEDIKGELAEDSGXXXDLISLAETTSKKKFSYNTSHSSSPFTRNISRDNSKKKSRPNQAPSRSYNPSHSQPSATSKSSKFNKQNEERYQWLVDERDAQRRPKSDPEYDPRTLYIPXSAWXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQRESMLAKEMREGSKGIVKRELQCILXXGTLXXXXXXXXXXXXXXXXXXXXXXXFYNETQLDXXXXVXXXXXXXXXXXXXXXXXXELQMLEFEDDSECTKLDTLMSQVRPMEVVMERNNLXXXXNKIXXXXXXXXXXXXXVKXGXXXXXXXKTXXXXISSEYFXTEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLFNRAITXXXXRMMKKWLXHPLXXXXXIEXXXXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXDVSKXXXXXXXXXXXXVKSWXXXFEXXKAINENIIVPQRGFDIEFDKSMDRIQELEXXXXXXXXXXXXXXXXXNIXYXXXXXXXXXXEIPIXXXXXXPSNXVQMXXXKXXXXXXSDEVXXLXXSMAEAKEIHKTXEEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXAPSCRPTIVDEVDSKTXXQLNGFLKFXXXXXXXFNXGATTAXXFIPNDIELGKEQPRXXLLTGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGANDXXXXXXXXFXXXXXXXXXXXXXXXXXXXXXVDELGXXXXSSDGFAXXEXXXXXXXXXXXXXXXXXXXXXXXXXSFKHHPXXRPLKMSILXXXXXXXXXXLYKXXXXXXXXXFXMHVAXXXXXXXXXIXXAQIAADNLEHTSRLVKERDLAANNLNGEVVSVPGXXXXXXXXIAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIDDLQS
>MSH6_YEAST__Q03834 RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;
MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKITKNPQGGKTGKLFVDVDEDNDLTIAEETVSTVRSDIMHSQEPQSDTMLNSNTTEPKSTTTDEDLSSSQSRRNHKRRVNYAESDDDDSDTTFTAKRKKGKVVDSESDEDEYLPDKNDGDEDDDIADDKEDIKGELAEDSGDDDDLISLAETTSKKKFSYNTSHSSSPFTRNISRDNSKKKSRPNQAPSRSYNPSHSQPSATSKSSKFNKQNEERYQWLVDERDAQRRPKSDPEYDPRTLYIPSSAWNKFTPFEKQYWEIKSKMWDCIVFFKKGKFFELYEKDALLANALFDLKIAGGGRANMQLAGIPEMSFEYWAAQFIQMGYKVAKVDQRESMLAKEMREGSKGIVKRELQCILTSGTLTDGDMLHSDLATFCLAIREEPGNFYNETQLDSSTIVQKLNTKIFGAAFIDTATGELQMLEFEDDSECTKLDTLMSQVRPMEVVMERNNLSTLANKIVKFNSAPNAIFNEVKAGEEFYDCDKTYAEIISSEYFSTEEDWPEVLKSYYDTGKKVGFSAFGGLLYYLKWLKLDKNLISMKNIKEYDFVKSQHSMVLDGITLQNLEIFSNSFDGSDKGTLFKLFNRAITPMGKRMMKKWLMHPLLRKNDIESRLDSVDSLLQDITLREQLEITFSKLPDLERMLARIHSRTIKVKDFEKVITAFETIIELQDSLKNNDLKGDVSKYISSFPEGLVEAVKSWTNAFERQKAINENIIVPQRGFDIEFDKSMDRIQELEDELMEILMTYRKQFKCSNIQYKDSGKEIYTIEIPISATKNVPSNWVQMAANKTYKRYYSDEVRALARSMAEAKEIHKTLEEDLKNRLCQKFDAHYNTIWMPTIQAISNIDCLLAITRTSEYLGAPSCRPTIVDEVDSKTNTQLNGFLKFKSLRHPCFNLGATTAKDFIPNDIELGKEQPRLGLLTGANAAGKSTILRMACIAVIMAQMGCYVPCESAVLTPIDRIMTRLGANDNIMQGKSTFFVELAETKKILDMATNRSLLVVDELGRGGSSSDGFAIAESVLHHVATHIQSLGFFATHYGTLASSFKHHPQVRPLKMSILVDEATRNVTFLYKMLEGQSEGSFGMHVASMCGISKEIIDNAQIAADNLEHTSRLVKERDLAANNLNGEVVSVPGGLQSDFVRIAYGDGLKNTKLGSGEGVLNYDWNIKRNVLKSLFSIIDDLQS
>RAD2_YEAST__P07276-slimfinder Motifs
----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------Q--I--FF-----------------------------
>RAD2_YEAST__P07276-masked
XGVHSFWDIAXPXXXXVRLESLEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRETIRQRKERRQGKRESAKSTARKLLALQLQNGSNDNVKNSTPXXGXSVQIFKPQDEWDLPDIPGFKYDKEDARVNSNKTFEKLMNSINGDGLEDIDLDTINPASAEFEEXPKXXXXXXXXXXXXXXXXXMXXXXEQLXTIXXXSXXXXXXXIXXXXXXXXFXQKLINTTGFQDGGASKLNEEVINRISGQKSKEYKLTKTNNGWILGLGANDXXDAQKAIVIDDKDAGALVKQLDSNAEDGDVLRWDDLEDNSLKIVRHESSNATTAPQKRSNRSEDEGCDSDECXWXXVELKPKNVKFVEDFSXKAARLPYMGQSLNNAGSKSFLDKRHDQASPSKTTPTMRISRISVEDDDEDYLKQIEEIEMMEAVQLSKMEKKPEADDKSKIAKPVTSKGTEARPPIVQYGLLGAQPDSKQPYHVTNLNSKSESVIKRTSKTVLSEFRPPSQQEDKGAILTEGEQNLNFISHKIPQFDFNNENSLLFQKNTESNVSQEATKEKSPIPEMPSWFSSTASQQLYNPYNTTNFVEDKNVRNEQESGAETTNKGSSYELLTGLNATEILERESEKESSNDENKDDDLEVLSEELFEDVPTKSQISKEAEDNDSRKVESINKEHRKPLIFDYDFSEDEEDNIVENMIKEQEEFDTFKNTTLSTSAERNVAENAFVEDELFEQQMKDKRDSDEVTMDMIKEXQXXXXXXXXXXXXXPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGXXXMXXXXXXXVXXEXXXXXNXKDWYNNGQFDKRKQETENKFEKDLRKKLVXNEIXXXXXXXXXXXXDAYMRPXXXXDTTPFVWXXXXXXXXXXFMKTQLGWPHEKSDEILIPLIRDVNKRXXXGXQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM
>RAD2_YEAST__P07276 RecName: Full=DNA repair protein RAD2; EC=3.1.-.-;
MGVHSFWDIAGPTARPVRLESLEDKRMAVDASIWIYQFLKAVRDQEGNAVKNSHITGFFRRICKLLYFGIRPVFVFDGGVPVLKRETIRQRKERRQGKRESAKSTARKLLALQLQNGSNDNVKNSTPSSGSSVQIFKPQDEWDLPDIPGFKYDKEDARVNSNKTFEKLMNSINGDGLEDIDLDTINPASAEFEELPKATQYLILSSLRLKSRLRMGYSKEQLETIFPNSMDFSRFQIDMVKRRNFFTQKLINTTGFQDGGASKLNEEVINRISGQKSKEYKLTKTNNGWILGLGANDGSDAQKAIVIDDKDAGALVKQLDSNAEDGDVLRWDDLEDNSLKIVRHESSNATTAPQKRSNRSEDEGCDSDECEWEEVELKPKNVKFVEDFSLKAARLPYMGQSLNNAGSKSFLDKRHDQASPSKTTPTMRISRISVEDDDEDYLKQIEEIEMMEAVQLSKMEKKPEADDKSKIAKPVTSKGTEARPPIVQYGLLGAQPDSKQPYHVTNLNSKSESVIKRTSKTVLSEFRPPSQQEDKGAILTEGEQNLNFISHKIPQFDFNNENSLLFQKNTESNVSQEATKEKSPIPEMPSWFSSTASQQLYNPYNTTNFVEDKNVRNEQESGAETTNKGSSYELLTGLNATEILERESEKESSNDENKDDDLEVLSEELFEDVPTKSQISKEAEDNDSRKVESINKEHRKPLIFDYDFSEDEEDNIVENMIKEQEEFDTFKNTTLSTSAERNVAENAFVEDELFEQQMKDKRDSDEVTMDMIKEVQELLSRFGIPYITAPMEAEAQCAELLQLNLVDGIITDDSDVFLFGGTKIYKNMFHEKNYVEFYDAESILKLLGLDRKNMIELAQLLGSDYTNGLKGMGPVSSIEVIAEFGNLKNFKDWYNNGQFDKRKQETENKFEKDLRKKLVNNEIILDDDFPSVMVYDAYMRPEVDHDTTPFVWGVPDLDMLRSFMKTQLGWPHEKSDEILIPLIRDVNKRKKKGKQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM
>RFC1_YEAST__P38630-slimfinder Motifs
---I--FF-K-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>RFC1_YEAST__P38630-masked
XVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLDTESDQESTNKTPKKMPVSNVIDVSETPEGEKKLPLPAKRKASSPTVKPASSKKTKPSXKXXDXASNITAQDVLDKIPSLDLSNVHVKENAKFDFKSANSNADPDEIVSEIGSFPEGKPXXXXXXXXXXXXXXXXXXXXAXXALAKRYGARVTXSXXXKTSVVVLGDEAGPKXLEKIKQLKIKAIDEEGFKQLIAGMPAEGGDGEAAEKARRKLEEQHNIATKEAELLVKKEEERSKKLAATRVSGGHLERDNVVREEDKLWTVKYAPTNLQQVCGNKGSVMKLKNWLANWENSKKNSFKHAGKDGSGVFRAAMLYGPPGIXKTTAAHXXXXXXXXXXXEQNXXDVRSKTLLNAGXKXXXXXXXVVGYFKHNEEAQXXNGKHFVIIMDEVDGMSGXDRXXVGQLAQFCXXXXXXXXXXCNERNXXXXXXXXXXXLDIXXXRXXXXSXKSRLMXXXXXXXXXXXXXXIDXXIXXXXXXXXXXINLLXXXSTXXKXINHENINEIXXAWXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQXXXXSTRPSVLKPGQSHLXXXAEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGFTRKYNSMTHPVAIYRTGSTIXXXXVGTSTSTPDFEDVVDADDNPVPADDEETQDSSTDLKKDKLIKQKAKPTKRKTATSKPGGSKKRKTKA
>RFC1_YEAST__P38630 RecName: Full=Replication factor C subunit 1; Short=Replication factor C1; AltName: Full=Activator 1 95 kDa subunit; AltName: Full=Cell division control protein 44;
MVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLDTESDQESTNKTPKKMPVSNVIDVSETPEGEKKLPLPAKRKASSPTVKPASSKKTKPSSKSSDSASNITAQDVLDKIPSLDLSNVHVKENAKFDFKSANSNADPDEIVSEIGSFPEGKPNCLLGLTIVFTGVLPTLERGASEALAKRYGARVTKSISSKTSVVVLGDEAGPKKLEKIKQLKIKAIDEEGFKQLIAGMPAEGGDGEAAEKARRKLEEQHNIATKEAELLVKKEEERSKKLAATRVSGGHLERDNVVREEDKLWTVKYAPTNLQQVCGNKGSVMKLKNWLANWENSKKNSFKHAGKDGSGVFRAAMLYGPPGIGKTTAAHLVAQELGYDILEQNASDVRSKTLLNAGVKNALDNMSVVGYFKHNEEAQNLNGKHFVIIMDEVDGMSGGDRGGVGQLAQFCRKTSTPLILICNERNLPKMRPFDRVCLDIQFRRPDANSIKSRLMTIAIREKFKLDPNVIDRLIQTTRGDIRQVINLLSTISTTTKTINHENINEISKAWEKNIALKPFDIAHKMLDGQIYSDIGSRNFTLNDKIALYFDDFDFTPLMIQENYLSTRPSVLKPGQSHLEAVAEAANCISLGDIVEKKIRSSEQLWSLLPLHAVLSSVYPASKVAGHMAGRINFTAWLGQNSKSAKYYRLLQEIHYHTRLGTSTDKIGLRLDYLPTFRKRLLDPFLKQGADAISSVIEVMDDYYLTKEDWDSIMEFFVGPDVTTAIIKKIPATVKSGFTRKYNSMTHPVAIYRTGSTIGGGGVGTSTSTPDFEDVVDADDNPVPADDEETQDSSTDLKKDKLIKQKAKPTKRKTATSKPGGSKKRKTKA
>RRM3_YEAST__P38766-slimfinder Motifs
---------------------------------RQ-TLSSFF---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------V--FY-------
>RRM3_YEAST__P38766-masked
XFRSHASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRNITAPPRPRLIRNNSXXLFXQSQGSFGDDDPDAEFKKLVDVPRLNSYKKSSRSLSMTSSLHKTASASTTQKTYHFDEDETLREVTSVKSNSRQLSFTSTINIEDSSMKLSTDSERPAKRSKPSMEFQGLKLTVPKKIKPLLRKTVSNMDSMNHRSASSPVVLTMEQERVVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIRKXXXXXGXXQXXLXXXXXXXXXXAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXAPXXLYATRREVEXXNVKKLXXXXXXXYEFKAVDXXXXXXXXILXXXXXXXXXXXXXXXXQXXXXXNKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXEXXEFRQXLNARXXXXXXXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXXXXXXXXXXXXXPRENXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXDXGKXXXNERVKDFYKRLETLK
>RRM3_YEAST__P38766 RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};
MFRSHASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRNITAPPRPRLIRNNSSSLFSQSQGSFGDDDPDAEFKKLVDVPRLNSYKKSSRSLSMTSSLHKTASASTTQKTYHFDEDETLREVTSVKSNSRQLSFTSTINIEDSSMKLSTDSERPAKRSKPSMEFQGLKLTVPKKIKPLLRKTVSNMDSMNHRSASSPVVLTMEQERVVNLIVKKRTNVFYTGSAGTGKSVILQTIIRQLSSLYGKESIAITASTGLAAVTIGGSTLHKWSGIGIGNKTIDQLVKKIQSQKDLLAAWRYTKVLIIDEISMVDGNLLDKLEQIARRIRKNDDPFGGIQLVLTGDFFQLPPVAKKDEHNVVKFCFESEMWKRCIQKTILLTKVFRQQDNKLIDILNAIRYGELTVDIAKTIRNLNRDIDYADGIAPTELYATRREVELSNVKKLQSLPGDLYEFKAVDNAPERYQAILDSSLMVEKVVALKEDAQVMMLKNKPDVELVNGSLGKVLFFVTESLVVKMKEIYKIVDDEVVMDMRLVSRVIGNPLLKESKEFRQDLNARPLARLERLKILINYAVKISPHKEKFPYVRWTVGKNKYIHELMVPERFPIDIPRENVGLERTQIPLMLCWALSIHKAQGQTIQRLKVDLRRIFEAGQVYVALSRAVTMDTLQVLNFDPGKIRTNERVKDFYKRLETLK
>UNG_HUMAN__P13051-slimfinder Motifs
---Q-TL-SFF--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>UNG_HUMAN__P13051-masked
XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESGDAAAIPAKKAPAGQEEPGTPPSSPLSAEQLDRIQRNKAAALLRLXXXXXXXXXXEXXXKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPXXXXXXXXQXXXXXXXXXXILGQDPYHGPNQAHGLCFSVQRPVXXXPSLENIYKELSTDIEDFVHPGHGDLSXWAKXXXXXXXXXXXXXAHQANSHKERGWEXFTDAVVXXXXXXXXXXXXXXXXXXXXXXGSAIDRKRHHVLQTAHPSPXXVYRGFFGXXXXSKTNELLQKSGKKPIDWKEL
>UNG_HUMAN__P13051 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESGDAAAIPAKKAPAGQEEPGTPPSSPLSAEQLDRIQRNKAAALLRLAARNVPVGFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL
>UNG_YEAST__P12887-slimfinder Motifs
-----------------K--Q-TI--FF--K----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>UNG_YEAST__P12887-masked
XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTETKAVAKEANTDKYPANSNAKDVYSKNLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFXXXXQADHTVFPPAXXXXXXXXXXXXXXXXXXXXGXDPXHXFNQAHGLAFSVKPXTXAXPSLKNIYKELKQEYPDFVEDNKVGDLXXWASXXXXXXNXSLTVRAHNANSHSKHGWETXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSXGSXXKYPNIMVMKSVHPXXLSASRGFFGXXXXXXXXXWXXXXXXXKMIDWSVVPGTSLREVQEANARLESESKDP
>UNG_YEAST__P12887 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;
MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTETKAVAKEANTDKYPANSNAKDVYSKNLSSNLRTLLSLELETIDDSWFPHLMDEFKKPYFVKLKQFVTKEQADHTVFPPAKDIYSWTRLTPFNKVKVVIIGQDPYHNFNQAHGLAFSVKPPTPAPPSLKNIYKELKQEYPDFVEDNKVGDLTHWASQGVLLLNTSLTVRAHNANSHSKHGWETFTKRVVQLLIQDREADGKSLVFLLWGNNAIKLVESLLGSTSVGSGSKYPNIMVMKSVHPSPLSASRGFFGTNHFKMINDWLYNTRGEKMIDWSVVPGTSLREVQEANARLESESKDP
>slimfinder 15120800001 SLiMFinder Motifs motifs
-01---------------------------------Q..[IL].SFF---------------------------XXXXXXXXXX-02---------------------------------Q.[ST]..SFF---------------------------XXXXXXXXXX-03---------------------------------Q.[ST][IL]..FF------------------------XXXXXXXXXX-04---------------------------------Q.TL..FF------------------------------XXXXXXXXXX-05---------------------------------Q..L..FF------------------------------XXXXXXXXXX-06---------------------------------[ST][IL].SFF------------------------XXXXXXXXXX-07---------------------------------TL.SFF------------------------------XXXXXXXXXX-08---------------------------------Q.[ST][IL].S.F------------------------XXXXXXXXXX-09---------------------------------Q.[ST][IL].SF------------------------XXXXXXXXXX-10---------------------------------Q..[IL]..FF---------------------------XXXXXXXXXX-11---------------------------------Q..I..FF..K------------------------------XXXXXXXXXX-12---------------------------------Q.T..SFF------------------------------XXXXXXXXXX-13---------------------------------[IL].SFF---------------------------XXXXXXXXXX-14---------------------------------TL.{0,1}S.{0,1}FF--------------------XXXXXXXXXX-15---------------------------------Q..L.SFF------------------------------XXXXXXXXXX-16---------------------------------Q..I..FF.{1,2}K--------------------------XXXXXXXXXX-17---------------------------------TL..FF------------------------------XXXXXXXXXX-18---------------------------------Q..[IL].S.F---------------------------XXXXXXXXXX-19---------------------------------Q..[IL].SF---------------------------XXXXXXXXXX-20---------------------------------K..Q..[IL]..FF---------------------------XXXXXXXXXX-21---------------------------------[ST]..SFF---------------------------XXXXXXXXXX-22---------------------------------[KR]Q..L..FF---------------------------XXXXXXXXXX-23---------------------------------Q.TL..F------------------------------XXXXXXXXXX-24---------------------------------Q.TL.S.F------------------------------XXXXXXXXXX-25---------------------------------T..SFF------------------------------XXXXXXXXXX-26---------------------------------Q.TL.SF------------------------------XXXXXXXXXX-27---------------------------------[ST][IL]..FF------------------------XXXXXXXXXX-28---------------------------------Q..I..FF------------------------------XXXXXXXXXX-29---------------------------------Q.[ST]..S.F---------------------------XXXXXXXXXX-30---------------------------------[KR]..TL..FF---------------------------XXXXXXXXXX-31---------------------------------Q.[ST]..SF---------------------------XXXXXXXXXX-32---------------------------------L.SFF------------------------------XXXXXXXXXX-33---------------------------------Q.T..S.F------------------------------XXXXXXXXXX-34---------------------------------I..FF.{1,2}K--------------------------XXXXXXXXXX-35---------------------------------Q.[ST][IL]..F------------------------XXXXXXXXXX-36---------------------------------[KR]Q.TL..F---------------------------XXXXXXXXXX-37---------------------------------Q.T.{1,2}S.{0,1}FF---------------------XXXXXXXXXX-38---------------------------------[ILM]..F[FY]-----------------------XXXXXXXXXX-39---------------------------------[IL]..FF---------------------------XXXXXXXXXX-40---------------------------------TL.S.F------------------------------XXXXXXXXXX-41---------------------------------TL.SF------------------------------XXXXXXXXXX-42---------------------------------I..FF..K------------------------------XXXXXXXXXX-43---------------------------------Q.SI..FF------------------------------XXXXXXXXXX-44---------------------------------Q.T.{1,2}S.F--------------------------XXXXXXXXXX-45---------------------------------Q.T..S.{0,1}F-------------------------XXXXXXXXXX-46---------------------------------L..FF------------------------------XXXXXXXXXX-47---------------------------------[ILMV]..F[FY]----------------------XXXXXXXXXX-48---------------------------------I..FF------------------------------XXXXXXXXXX-49---------------------------------KQ..L..FF------------------------------XXXXXXXXXX-50---------------------------------Q..L..F------------------------------
>DNLI1_YEAST__P04819 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0038-CLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0038-CLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0038-CLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0038-CLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0040-LSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0035-LTGCLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0037-GCLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0038-CLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDN-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0040-LSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0037-GCLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0038-CLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDN-XXXXXXXXXX-0037-GCLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDN-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0041-SSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0041-SSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0041-SSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0041-SSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0037-GCLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0038-CLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDN-
>RRM3_YEAST__P38766 RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};
-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRNI-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0034-SHASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0034-SHASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0034-SHASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRNI-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-
>RRM3_YEAST__P38766 RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0712-QVYVALSRAVTMDTLQVLNFDPGKIRTNERVKDFYKRLETLK-----------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>MSH3_YEAST__P25336 RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLDTD-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0006--------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX-0004----------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0007-------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLDTD-XXXXXXXXXX-0004----------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESIC-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLD-XXXXXXXXXX-0007-------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX-0007-------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0007-------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX-0007-------------------------MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>FEN1_YEAST__P26793 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0340-IEYLCDDKKFSEERVKSGISRLKKGLKSGIQGRLDGFFQVVPKTKEQLAAAAKRAQENKKLNKNKNK-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0340-IEYLCDDKKFSEERVKSGISRLKKGLKSGIQGRLDGFFQVVPKTKEQLAAAAKRAQENKKLNKNKNK-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0343-LCDDKKFSEERVKSGISRLKKGLKSGIQGRLDGFFQVVPKTKEQLAAAAKRAQENKKLNKNKNK-XXXXXXXXXX-0343-LCDDKKFSEERVKSGISRLKKGLKSGIQGRLDGFFQVVPKTKEQLAAAAKRAQENKKLNKNKNK-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0343-LCDDKKFSEERVKSGISRLKKGLKSGIQGRLDGFFQVVPKTKEQLAAAAKRAQENKKLNKNKNK-XXXXXXXXXX-0343-LCDDKKFSEERVKSGISRLKKGLKSGIQGRLDGFFQVVPKTKEQLAAAAKRAQENKKLNKNKNK-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0340-IEYLCDDKKFSEERVKSGISRLKKGLKSGIQGRLDGFFQVVPKTKEQLAAAAKRAQENKKLNKNKN-
>FEN1_YEAST__P26793 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0066-SMSLYQFLIAVRQQDGGQLTNEAGETTSHLMGMFYRTLRMIDNGIKPCYVFDGKPPDLKSHELT-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0066-SMSLYQFLIAVRQQDGGQLTNEAGETTSHLMGMFYRTLRMIDNGIKPCYVFDGKPPDLKSHELT-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>FEN1_HUMAN__P39748 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0337-IKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0337-IKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0340-MCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX-0340-MCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0340-MCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX-0340-MCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0337-IKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGA-
>FEN1_HUMAN__P39748 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0065-ASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELA-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0065-ASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELA-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DNMT1_HUMAN__P26358 RecName: Full=DNA (cytosine-5)-methyltransferase 1; Short=Dnmt1; EC=2.1.1.37; AltName: Full=CXXC-type zinc finger protein 9; AltName: Full=DNA methyltransferase HsaI; Short=DNA MTase HsaI; Short=M.HsaI; AltName: Full=MCMT;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0164-KPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQ-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0164-KPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQ-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0164-KPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQ-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0164-KPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQ-XXXXXXXXXX-0164-KPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQ-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-1018-PEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYWSDEEAVV-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>ERCC5_HUMAN__P28715 RecName: Full=DNA repair protein complementing XP-G cells; EC=3.1.-.-; AltName: Full=DNA excision repair protein ERCC-5; AltName: Full=Xeroderma pigmentosum group G-complementing protein;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0993-QRYFGWNRTKTDESLFPVLKQLDAQQTQLRIDSFFRLAQQEKEDAKRIKSQRLNRAVTCMLRKE-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0993-QRYFGWNRTKTDESLFPVLKQLDAQQTQLRIDSFFRLAQQEKEDAKRIKSQRLNRAVTCMLRKE-XXXXXXXXXX-0993-QRYFGWNRTKTDESLFPVLKQLDAQQTQLRIDSFFRLAQQEKEDAKRIKSQRLNRAVTCMLRKE-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0993-QRYFGWNRTKTDESLFPVLKQLDAQQTQLRIDSFFRLAQQEKEDAKRIKSQRLNRAVTCMLRKE-XXXXXXXXXX-0993-QRYFGWNRTKTDESLFPVLKQLDAQQTQLRIDSFFRLAQQEKEDAKRIKSQRLNRAVTCMLRKE-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>UNG_YEAST__P12887 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0021-----------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0021-----------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX-0021-----------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTE-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0021-----------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTE-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0018--------------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0023---------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX-0021-----------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0024--------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTE-XXXXXXXXXX-0021-----------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0024--------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX-0024--------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0024--------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTE-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0024--------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX-0024--------MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>RFC1_YEAST__P38630 RecName: Full=Replication factor C subunit 1; Short=Replication factor C1; AltName: Full=Activator 1 95 kDa subunit; AltName: Full=Cell division control protein 44;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLDTES-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLD-XXXXXXXXXX-0004----------------------------MVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLD-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLD-XXXXXXXXXX-0004----------------------------MVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLD-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>UNG_HUMAN__P13051 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0007-------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESG-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0006--------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0006--------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX-0006--------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX-0007-------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESG-XXXXXXXXXX-0007-------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0007-------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0007-------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0007-------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-
>UNG_HUMAN__P13051 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DPOD3_SCHPO__P30261 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;
-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0364-GTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK--------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK--------------------------XXXXXXXXXX-0359-ENISTGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0364-GTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0364-GTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK--------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK--------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DPOD3_SCHPO__P30261 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DPOD3_YEAST__P47110 RecName: Full=DNA polymerase delta subunit 3;
-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK--------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0337-TPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0337-TPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0337-TPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK--------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0337-TPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------
>DPOD3_YEAST__P47110 RecName: Full=DNA polymerase delta subunit 3;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>MSH6_YEAST__Q03834 RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;
-0027-----MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0027-----MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0027-----MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0027-----MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0030--MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0027-----MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0027-----MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0027-----MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDK-XXXXXXXXXX-0024--------MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0029---MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0026------MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0027-----MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0027-----MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDK-XXXXXXXXXX-0030--MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0030--MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0030--MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0030--MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0030--MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0026------MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0027-----MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDK-
>CDN1A_HUMAN__P38936 RecName: Full=Cyclin-dependent kinase inhibitor 1; AltName: Full=CDK-interacting protein 1; AltName: Full=Melanoma differentiation-associated protein 6; Short=MDA-6; AltName: Full=p21;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0147-CTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP-----------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0147-CTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP-----------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DPOD3_HUMAN__Q15054 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0458-PAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK------------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK--------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK------------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>MSH6_HUMAN__P52701 RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;
-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0006--------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0006--------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPG-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0007-------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0006--------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGAS-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0006--------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPG-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0006--------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0003-----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPG-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0006--------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPG-XXXXXXXXXX-0006--------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0003-----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPG-XXXXXXXXXX-0007-------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPG-XXXXXXXXXX-0003-----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPG-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGAS-XXXXXXXXXX-0007-------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0007-------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0006--------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0006--------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPG-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0007-------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-0007-------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPG-
>MSH6_HUMAN__P52701 RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGA-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>RAD2_YEAST__P07276 RecName: Full=DNA repair protein RAD2; EC=3.1.-.-;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0995-KTQLGWPHEKSDEILIPLIRDVNKRKKKGKQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0995-KTQLGWPHEKSDEILIPLIRDVNKRKKKGKQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0998-LGWPHEKSDEILIPLIRDVNKRKKKGKQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX-0998-LGWPHEKSDEILIPLIRDVNKRKKKGKQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0998-LGWPHEKSDEILIPLIRDVNKRKKKGKQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX-0998-LGWPHEKSDEILIPLIRDVNKRKKKGKQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DNLI1_HUMAN__P18858 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0227-TESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKA-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKE-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0005---------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0227-TESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPLD-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKE-XXXXXXXXXX-0227-TESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKA-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0227-TESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKA-XXXXXXXXXX-0228-ESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0005---------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKE-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0005---------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0005---------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0227-TESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-0227-TESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGP-XXXXXXXXXX-0005---------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKE-XXXXXXXXXX-0002------------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0228-ESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-0005---------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0005---------------------------MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAA-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DNLI1_HUMAN__P18858 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0227-TESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0228-ESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0227-TESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0227-TESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0228-ESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-0228-ESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0228-ESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>slimfinder 15120800001 SLiMFinder Motifs motifs
-01---------------------------------Q..[IL].SFF---------------------------XXXXXXXXXX-02---------------------------------Q.[ST]..SFF---------------------------XXXXXXXXXX-03---------------------------------Q.[ST][IL]..FF------------------------XXXXXXXXXX-04---------------------------------Q.TL..FF------------------------------XXXXXXXXXX-05---------------------------------Q..L..FF------------------------------XXXXXXXXXX-06---------------------------------[ST][IL].SFF------------------------XXXXXXXXXX-07---------------------------------TL.SFF------------------------------XXXXXXXXXX-08---------------------------------Q.[ST][IL].S.F------------------------XXXXXXXXXX-09---------------------------------Q.[ST][IL].SF------------------------XXXXXXXXXX-10---------------------------------Q..[IL]..FF---------------------------XXXXXXXXXX-11---------------------------------Q..I..FF..K------------------------------XXXXXXXXXX-12---------------------------------Q.T..SFF------------------------------XXXXXXXXXX-13---------------------------------[IL].SFF---------------------------XXXXXXXXXX-14---------------------------------TL.{0,1}S.{0,1}FF--------------------XXXXXXXXXX-15---------------------------------Q..L.SFF------------------------------XXXXXXXXXX-16---------------------------------Q..I..FF.{1,2}K--------------------------XXXXXXXXXX-17---------------------------------TL..FF------------------------------XXXXXXXXXX-18---------------------------------Q..[IL].S.F---------------------------XXXXXXXXXX-19---------------------------------Q..[IL].SF---------------------------XXXXXXXXXX-20---------------------------------K..Q..[IL]..FF---------------------------XXXXXXXXXX-21---------------------------------[ST]..SFF---------------------------XXXXXXXXXX-22---------------------------------[KR]Q..L..FF---------------------------XXXXXXXXXX-23---------------------------------Q.TL..F------------------------------XXXXXXXXXX-24---------------------------------Q.TL.S.F------------------------------XXXXXXXXXX-25---------------------------------T..SFF------------------------------XXXXXXXXXX-26---------------------------------Q.TL.SF------------------------------XXXXXXXXXX-27---------------------------------[ST][IL]..FF------------------------XXXXXXXXXX-28---------------------------------Q..I..FF------------------------------XXXXXXXXXX-29---------------------------------Q.[ST]..S.F---------------------------XXXXXXXXXX-30---------------------------------[KR]..TL..FF---------------------------XXXXXXXXXX-31---------------------------------Q.[ST]..SF---------------------------XXXXXXXXXX-32---------------------------------L.SFF------------------------------XXXXXXXXXX-33---------------------------------Q.T..S.F------------------------------XXXXXXXXXX-34---------------------------------I..FF.{1,2}K--------------------------XXXXXXXXXX-35---------------------------------Q.[ST][IL]..F------------------------XXXXXXXXXX-36---------------------------------[KR]Q.TL..F---------------------------XXXXXXXXXX-37---------------------------------Q.T.{1,2}S.{0,1}FF---------------------XXXXXXXXXX-38---------------------------------[ILM]..F[FY]-----------------------XXXXXXXXXX-39---------------------------------[IL]..FF---------------------------XXXXXXXXXX-40---------------------------------TL.S.F------------------------------XXXXXXXXXX-41---------------------------------TL.SF------------------------------XXXXXXXXXX-42---------------------------------I..FF..K------------------------------XXXXXXXXXX-43---------------------------------Q.SI..FF------------------------------XXXXXXXXXX-44---------------------------------Q.T.{1,2}S.F--------------------------XXXXXXXXXX-45---------------------------------Q.T..S.{0,1}F-------------------------XXXXXXXXXX-46---------------------------------L..FF------------------------------XXXXXXXXXX-47---------------------------------[ILMV]..F[FY]----------------------XXXXXXXXXX-48---------------------------------I..FF------------------------------XXXXXXXXXX-49---------------------------------KQ..L..FF------------------------------XXXXXXXXXX-50---------------------------------Q..L..F------------------------------
>DNLI1_YEAST__P04819 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0038-CLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0038-CLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0038-CLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0038-CLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0040-LSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0035-LTGCLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0037-GCLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0038-CLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDN-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0040-LSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0037-GCLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0038-CLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDN-XXXXXXXXXX-0037-GCLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDN-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0041-SSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0041-SSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0041-SSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0041-SSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0037-GCLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNV-XXXXXXXXXX-0038-CLLSSAXPLKSRLPLLMSXXLPXSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDN-
>RRM3_YEAST__P38766 RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};
-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRNI-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0034-SHASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0034-SHASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0034-SHASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRNI-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0037-SGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0038-GNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNR-
>RRM3_YEAST__P38766 RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-0035-HASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRN-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0712-XXXXXXXXXXXXXXXXXXXXDXGKXXXNERVKDFYKRLETLK-----------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>MSH3_YEAST__P25336 RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLDTD-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0006--------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX-0004----------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0007-------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLDTD-XXXXXXXXXX-0004----------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESIC-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLD-XXXXXXXXXX-0007-------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX-0007-------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0007-------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX-0007-------------------------XXGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICL-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>FEN1_YEAST__P26793 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0340-IEYLCDDKKXSEERVKSGISRLKKGLKSGIQXRLDGFFQVVPKTKEQLAXXXKRAQENKKLNKNKNK-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0340-IEYLCDDKKXSEERVKSGISRLKKGLKSGIQXRLDGFFQVVPKTKEQLAXXXKRAQENKKLNKNKNK-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0343-LCDDKKXSEERVKSGISRLKKGLKSGIQXRLDGFFQVVPKTKEQLAXXXKRAQENKKLNKNKNK-XXXXXXXXXX-0343-LCDDKKXSEERVKSGISRLKKGLKSGIQXRLDGFFQVVPKTKEQLAXXXKRAQENKKLNKNKNK-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0343-LCDDKKXSEERVKSGISRLKKGLKSGIQXRLDGFFQVVPKTKEQLAXXXKRAQENKKLNKNKNK-XXXXXXXXXX-0343-LCDDKKXSEERVKSGISRLKKGLKSGIQXRLDGFFQVVPKTKEQLAXXXKRAQENKKLNKNKNK-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0340-IEYLCDDKKXSEERVKSGISRLKKGLKSGIQXRLDGFFQVVPKTKEQLAXXXKRAQENKKLNKNKN-
>FEN1_YEAST__P26793 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0066-XXXXXXXXXXXXXXDGGQLTNEAGETTSHLMGMFYXXLXXXXXXXKPCYVFDGKPPDLKSHELT-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0066-XXXXXXXXXXXXXXDGGQLTNEAGETTSHLMGMFYXXLXXXXXXXKPCYVFDGKPPDLKSHELT-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>FEN1_HUMAN__P39748 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0337-IKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0337-IKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0340-MCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX-0340-MCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0340-MCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX-0340-MCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAA-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0337-IKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGA-
>FEN1_HUMAN__P39748 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0065-XXXXXXXXXXXXXXXXDVLQNEEGETTSHLMGMFYRTIXXXXXXIKPVYVFDGKPPQLKSGELA-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0065-XXXXXXXXXXXXXXXXDVLQNEEGETTSHLMGMFYRTIXXXXXXIKPVYVFDGKPPQLKSGELA-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DNMT1_HUMAN__P26358 RecName: Full=DNA (cytosine-5)-methyltransferase 1; Short=Dnmt1; EC=2.1.1.37; AltName: Full=CXXC-type zinc finger protein 9; AltName: Full=DNA methyltransferase HsaI; Short=DNA MTase HsaI; Short=M.HsaI; AltName: Full=MCMT;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0164-KPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQ-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0164-KPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQ-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0164-KPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQ-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0164-KPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQ-XXXXXXXXXX-0164-KPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQ-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-1018-PEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINXXXXXXXXXXX-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>ERCC5_HUMAN__P28715 RecName: Full=DNA repair protein complementing XP-G cells; EC=3.1.-.-; AltName: Full=DNA excision repair protein ERCC-5; AltName: Full=Xeroderma pigmentosum group G-complementing protein;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0993-XXXFGXXXXXXXXXLFPVLKQXXXXXTXXRIDSFFRLAXQEKEDAKRIKSQRLNRAVTCMLRKE-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0993-XXXFGXXXXXXXXXLFPVLKQXXXXXTXXRIDSFFRLAXQEKEDAKRIKSQRLNRAVTCMLRKE-XXXXXXXXXX-0993-XXXFGXXXXXXXXXLFPVLKQXXXXXTXXRIDSFFRLAXQEKEDAKRIKSQRLNRAVTCMLRKE-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0993-XXXFGXXXXXXXXXLFPVLKQXXXXXTXXRIDSFFRLAXQEKEDAKRIKSQRLNRAVTCMLRKE-XXXXXXXXXX-0993-XXXFGXXXXXXXXXLFPVLKQXXXXXTXXRIDSFFRLAXQEKEDAKRIKSQRLNRAVTCMLRKE-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>UNG_YEAST__P12887 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0021-----------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0021-----------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX-0021-----------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTE-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0021-----------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTE-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0018--------------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0023---------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX-0021-----------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0024--------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTE-XXXXXXXXXX-0021-----------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0024--------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX-0024--------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0024--------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTE-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0024--------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX-0024--------XWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAI-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>RFC1_YEAST__P38630 RecName: Full=Replication factor C subunit 1; Short=Replication factor C1; AltName: Full=Activator 1 95 kDa subunit; AltName: Full=Cell division control protein 44;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLDTES-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLD-XXXXXXXXXX-0004----------------------------XVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLD-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLD-XXXXXXXXXX-0004----------------------------XVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLD-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>UNG_HUMAN__P13051 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0007-------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESG-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0006--------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0006--------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX-0006--------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX-0007-------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESG-XXXXXXXXXX-0007-------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0007-------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0006--------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0007-------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-0007-------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEE-
>UNG_HUMAN__P13051 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEES-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DPOD3_SCHPO__P30261 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;
-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0364-GTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK--------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK--------------------------XXXXXXXXXX-0359-ENISTGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0364-GTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0364-GTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK--------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK--------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK---------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DPOD3_SCHPO__P30261 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0362-STGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0365-TSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DPOD3_YEAST__P47110 RecName: Full=DNA polymerase delta subunit 3;
-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK--------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0337-TPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0337-TPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0337-TPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK--------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0340-RKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0341-KPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0337-TPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK------------------------
>DPOD3_YEAST__P47110 RecName: Full=DNA polymerase delta subunit 3;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0338-PPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK-------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>MSH6_YEAST__Q03834 RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;
-0027-----XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0027-----XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0027-----XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0027-----XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0030--XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0027-----XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0027-----XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0027-----XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDK-XXXXXXXXXX-0024--------XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0029---XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0026------XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0027-----XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0027-----XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDK-XXXXXXXXXX-0030--XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0030--XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0030--XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0030--XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0030--XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0026------XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKI-XXXXXXXXXX-0027-----XXPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDK-
>CDN1A_HUMAN__P38936 RecName: Full=Cyclin-dependent kinase inhibitor 1; AltName: Full=CDK-interacting protein 1; AltName: Full=Melanoma differentiation-associated protein 6; Short=MDA-6; AltName: Full=p21;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0147-CTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP-----------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0147-CTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP-----------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DPOD3_HUMAN__Q15054 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0458-PAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK------------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK--------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK------------------------------XXXXXXXXXX-0456-RPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX-0459-AMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK---------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>MSH6_HUMAN__P52701 RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;
-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0006--------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0006--------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPG-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0007-------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0006--------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGAS-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0006--------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPG-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0006--------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0003-----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPG-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0006--------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPG-XXXXXXXXXX-0006--------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0003-----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPG-XXXXXXXXXX-0007-------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPG-XXXXXXXXXX-0003-----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPG-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGAS-XXXXXXXXXX-0007-------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0007-------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0006--------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0006--------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPG-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0007-------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-0007-------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPG-
>MSH6_HUMAN__P52701 RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XSRQSTLYSFFPKSPALSDANKASARASREGGRAXXXPGA-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>RAD2_YEAST__P07276 RecName: Full=DNA repair protein RAD2; EC=3.1.-.-;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0995-KTQLGWPHEKSDEILIPLIRDVNKRXXXGXQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0995-KTQLGWPHEKSDEILIPLIRDVNKRXXXGXQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0998-LGWPHEKSDEILIPLIRDVNKRXXXGXQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX-0998-LGWPHEKSDEILIPLIRDVNKRXXXGXQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0998-LGWPHEKSDEILIPLIRDVNKRXXXGXQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX-0998-LGWPHEKSDEILIPLIRDVNKRXXXGXQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DNLI1_HUMAN__P18858 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0227-TESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKA-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAALKE-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0005---------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0227-TESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPLD-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAALKE-XXXXXXXXXX-0227-TESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKA-XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0227-TESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0004----------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKA-XXXXXXXXXX-0228-ESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0005---------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAALKE-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0005---------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0005---------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0227-TESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-0227-TESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGP-XXXXXXXXXX-0005---------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAALKE-XXXXXXXXXX-0002------------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0228-ESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-0005---------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX-0005---------------------------XQRSIMSFFHPKXEGXAXKPEKEASNSSRETEPPPKAA-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>DNLI1_HUMAN__P18858 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0227-TESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-0228-ESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------------XXXXXXXXXX-0227-TESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0227-TESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-0228-ESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-0228-ESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX--------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-0228-ESVSEPEVATKQELQXXXEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPL-XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX---------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------
>CDN1A_HUMAN__P38936 RecName: Full=Cyclin-dependent kinase inhibitor 1; AltName: Full=CDK-interacting protein 1; AltName: Full=Melanoma differentiation-associated protein 6; Short=MDA-6; AltName: Full=p21;
MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP
>DNLI1_HUMAN__P18858 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKEWNGVVSESDSPVKRPGRKAARVLGSEGEEEDEALSPAKGQKPALDCSQVSPPRPATSPENNASLSDTSPMDSSPSGIPKRRTARKQLPKRTIQEVLEEQSEDEDREAKRKKEEEEEETPKESLTEAEVATEKEGEDGDQPTTPPKPLKTSKAETPTESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPLDPSGYNPAKNNYHPVEDACWKPGQKVPYLAVARTFEKIEEVSARLRMVETLSNLLRSVVALSPPDLLPVLYLSLNHLGPPQQGLELGVGDGVLLKAVAQATGRQLESVRAEAAEKGDVGLVAENSRSTQRLMLPPPPLTASGVFSKFRDIARLTGSASTAKKIDIIKGLFVACRHSEARFIARSLSGRLRLGLAEQSVLAALSQAVSLTPPGQEFPPAMVDAGKGKTAEARKTWLEEQGMILKQTFCEVPDLDRIIPVLLEHGLERLPEHCKLSPGIPLKPMLAHPTRGISEVLKRFEEAAFTCEYKYDGQRAQIHALEGGEVKIFSRNQEDNTGKYPDIISRIPKIKLPSVTSFILDTEAVAWDREKKQIQPFQVLTTRKRKEVDASEIQVQVCLYAFDLIYLNGESLVREPLSRRRQLLRENFVETEGEFVFATSLDTKDIEQIAEFLEQSVKDSCEGLMVKTLDVDATYEIAKRSHNWLKLKKDYLDGVGDTLDLVVIGAYLGRGKRAGRYGGFLLASYDEDSEELQAICKLGTGFSDEELEEHHQSLKALVLPSPRPYVRIDGAVIPDHWLDPSAVWEVKCADLSLSPIYPAARGLVDSDKGISLRFPRFIRVREDKQPEQATTSAQVACLYRKQSQIQNQQGEDSGSDPEDTY
>DNLI1_YEAST__P04819 RecName: Full=DNA ligase 1; EC=6.5.1.1; AltName: Full=DNA ligase I; AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; Flags: Precursor;
MRRLLTGCLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNVSGEEEYATKKLKQTAVTHTVAAPSSMGSNFSSIPSSAPSSGVADSPQQSQRLVGEVEDALSSNNNDHYSSNIPYSEVCEVFNKIEAISSRLEIIRICSDFFIKIMKQSSKNLIPTTYLFINRLGPDYEAGLELGLGENLLMKTISETCGKSMSQIKLKYKDIGDLGEIAMGARNVQPTMFKPKPLTVGEVFKNLRAIAKTQGKDSQLKKMKLIKRMLTACKGIEAKFLIRSLESKLRIGLAEKTVLISLSKALLLHDENREDSPDKDVPMDVLESAQQKIRDAFCQVPNYEIVINSCLEHGIMNLDKYCTLRPGIPLKPMLAKPTKAINEVLDRFQGETFTSEYKYDGERAQVHLLNDGTMRIYSRNGENMTERYPEINITDFIQDLDTTKNLILDCEAVAWDKDQGKILPFQVLSTRKRKDVELNDVKVKVCLFAFDILCYNDERLINKSLKERREYLTKVTKVVPGEFQYATQITTNNLDELQKFLDESVNHSCEGLMVKMLEGPESHYEPSKRSRNWLKLKKDYLEGVGDSLDLCVLGAYYGRGKRTGTYGGFLLGCYNQDTGEFETCCKIGTGFSDEMLQLLHDRLTPTIIDGPKATFVFDSSAEPDVWFEPTTLFEVLTADLSLSPIYKAGSATFDKGVSLRFPRFLRIREDKGVEDATSSDQIVELYENQSHMQN
>DNMT1_HUMAN__P26358 RecName: Full=DNA (cytosine-5)-methyltransferase 1; Short=Dnmt1; EC=2.1.1.37; AltName: Full=CXXC-type zinc finger protein 9; AltName: Full=DNA methyltransferase HsaI; Short=DNA MTase HsaI; Short=M.HsaI; AltName: Full=MCMT;
MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQLCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEKEEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGLNLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQQPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQGKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLAEMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD
>DPOD3_HUMAN__Q15054 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=DNA polymerase delta subunit p66;
MADQLYLENIDEFVTDQNKIVTYKWLSYTLGVHVNQAKQMLYDYVERKRKENSGAQLHVTYLVSGSLIQNGHSCHKVAVVREDKLEAVKSKLAVTASIHVYSIQKAMLKDSGPLFNTDYDILKSNLQNCSKFSAIQCAAAVPRAPAESSSSSKKFEQSHLHMSSETQANNELTTNGHGPPASKQVSQQPKGIMGMFASKAAAKTQETNKETKTEAKEVTNASAAGNKAPGKGNMMSNFFGKAAMNKFKVNLDSEQAVKEEKIVEQPTVSVTEPKLATPAGLKKSSKKAEPVKVLQKEKKRGKRVALSDDETKETENMRKKRRRIKLPESDSSEDEVFPDSPGAYEAESPSPPPPPSPPLEPVPKTEPEPPSVKSSSGENKRKRKRVLKSKTYLDGEGCIVTEKVYESESCTDSEEELNMKTSSVHRPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK
>DPOD3_YEAST__P47110 RecName: Full=DNA polymerase delta subunit 3;
MDQKASYFINEKLFTEVKPVLFTDLIHHLKIGPSMAKKLMFDYYKQTTNAKYNCVVICCYKDQTIKIIHDLSNIPQQDSIIDCFIYAFNPMDSFIPYYDIIDQKDCLTIKNSYELKVSESSKIIERTKTLEEKSKPLVRPTARSKTTPEETTGRKSKSKDMGLRSTALLAKMKKDRDDKETSRQNELRKRKEENLQKINKQNPEREAQMKELNNLFVEDDLDTEEVNGGSKPNSPKETDSNDKDKNNDDLEDLLETTAEDSLMDVPKIQQTKPSETEHSKEPKSEEEPSSFIDEDGYIVTKRPATSTPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK
>DPOD3_SCHPO__P30261 RecName: Full=DNA polymerase delta subunit 3; AltName: Full=Cell division control protein 27;
MEEWRNFLDIKVINESSLVTVDNLSLQLDISSEKAQEYLNMFYQGNDFLYPIYLIHGQPIDDEINLEIDEESQPISNFPVLQYILCDKSSLQEKQSRLKSGYKTVIFALSSAPLSDFDELLPAVYEIREKDVLYKKEDADKYGFIFNENSVPRVLKKAPSTHSPQLSVPSKTSTIDKTDTRSTEKTKGKDIFSNARNQKGNSSRKNKKAPLENHKEKEPLLPKEEKLSEQAKRERDDLKNIMQLEDESVSTTSVHDSEDDNLDSNNFQLEIGTEAKSAAPDEPQEIIKSVSGGKRRGKRKVKKYATTKDEEGFLVTKEEEVWESFSEDENISTGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK
>ERCC5_HUMAN__P28715 RecName: Full=DNA repair protein complementing XP-G cells; EC=3.1.-.-; AltName: Full=DNA excision repair protein ERCC-5; AltName: Full=Xeroderma pigmentosum group G-complementing protein;
MGVQGLWKLLECSGRQVSPEALEGKILAVDISIWLNQALKGVRDRHGNSIENPHLLTLFHRLCKLLFFRIRPIFVFDGDAPLLKKQTLVKRRQRKDLASSDSRKTTEKLLKTFLKRQAIKTAFRSKRDEALPSLTQVRRENDLYVLPPLQEEEKHSSEEEDEKEWQERMNQKQALQEEFFHNPQAIDIESEDFSSLPPEVKHEILTDMKEFTKRRRTLFEAMPEESDDFSQYQLKGLLKKNYLNQHIEHVQKEMNQQHSGHIRRQYEDEGGFLKEVESRRVVSEDTSHYILIKGIQAKTVAEVDSESLPSSSKMHGMSFDVKSSPCEKLKTEKEPDATPPSPRTLLAMQAALLGSSSEEELESENRRQARGRNAPAAVDEGSISPRTLSAIKRALDDDEDVKVCAGDDVQTGGPGAEEMRINSSTENSDEGLKVRDGKGIPFTATLASSSVNSAEEHVASTNEGREPTDSVPKEQMSLVHVGTEAFPISDESMIKDRKDRLPLESAVVRHSDAPGLPNGRELTPASPTCTNSVSKNETHAEVLEQQNELCPYESKFDSSLLSSDDETKCKPNSASEVIGPVSLQETSSIVSVPSEAVDNVENVVSFNAKEHENFLETIQEQQTTESAGQDLISIPKAVEPMEIDSEESESDGSFIEVQSVISDEELQAEFPETSKPPSEQGEEELVGTREGEAPAESESLLRDNSERDDVDGEPQEAEKDAEDSLHEWQDINLEELETLESNLLAQQNSLKAQKQQQERIAATVTGQMFLESQELLRLFGIPYIQAPMEAEAQCAILDLTDQTSGTITDDSDIWLFGARHVYRNFFNKNKFVEYYQYVDFHNQLGLDRNKLINLAYLLGSDYTEGIPTVGCVTAMEILNEFPGHGLEPLLKFSEWWHEAQKNPKIRPNPHDTKVKKKLRTLQLTPGFPNPAVAEAYLKPVVDDSKGSFLWGKPDLDKIREFCQRYFGWNRTKTDESLFPVLKQLDAQQTQLRIDSFFRLAQQEKEDAKRIKSQRLNRAVTCMLRKEKEAAASEIEAVSVAMEKEFELLDKAKGKTQKRGITNTLEESSSLKRKRLSDSKGKNTCGGFLGETCLSESSDGSSSEDAESSSLMNVQRRTAAKEPKTSASDSQNSVKEAPVKNGGATTSSSSDSDDDGGKEKMVLVTARSVFGKKRRKLRRARGRKRKT
>FEN1_HUMAN__P39748 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=DNase IV; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Maturation factor 1; Short=MF1; Short=hFEN-1;
MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK
>FEN1_YEAST__P26793 RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}; EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}; AltName: Full=RAD2 homolog nuclease 1; Short=RTH1 nuclease; AltName: Full=Structure-specific endonuclease RAD27;
MGIKGLNAIISEHVPSAIRKSDIKSFFGRKVAIDASMSLYQFLIAVRQQDGGQLTNEAGETTSHLMGMFYRTLRMIDNGIKPCYVFDGKPPDLKSHELTKRSSRRVETEKKLAEATTELEKMKQERRLVKVSKEHNEEAQKLLGLMGIPYIIAPTEAEAQCAELAKKGKVYAAASEDMDTLCYRTPFLLRHLTFSEAKKEPIHEIDTELVLRGLDLTIEQFVDLCIMLGCDYCESIRGVGPVTALKLIKTHGSIEKIVEFIESGESNNTKWKIPEDWPYKQARMLFLDPEVIDGNEINLKWSPPKEKELIEYLCDDKKFSEERVKSGISRLKKGLKSGIQGRLDGFFQVVPKTKEQLAAAAKRAQENKKLNKNKNKVTKGRR
>MSH3_YEAST__P25336 RecName: Full=DNA mismatch repair protein MSH3; AltName: Full=Mismatch-binding protein; Short=MBP; AltName: Full=MutS protein homolog 3;
MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLDTDEEDNLSSVASTTVTNDSFPLKGSVSSKNSKNSEKTSGTSTTFNDIDFAKKLDRIMKRRSDENVEAEDDEEEGEEDFVKKKARKSPTAKLTPLDKQVKDLKMHHRDKVLVIRVGYKYKCFAEDAVTVSRILHIKLVPGKLTIDESNPQDCNHRQFAYCSFPDVRLNVHLERLVHHNLKVAVVEQAETSAIKKHDPGASKSSVFERKISNVFTKATFGVNSTFVLRGKRILGDTNSIWALSRDVHQGKVAKYSLISVNLNNGEVVYDEFEEPNLADEKLQIRIKYLQPIEVLVNTDDLPLHVAKFFKDISCPLIHKQEYDLEDHVVQAIKVMNEKIQLSPSLIRLVSKLYSHMVEYNNEQVMLIPSIYSPFASKIHMLLDPNSLQSLDIFTHDGGKGSLFWLLDHTRTSFGLRMLREWILKPLVDVHQIEERLDAIECITSEINNSIFFESLNQMLNHTPDLLRTLNRIMYGTTSRKEVYFYLKQITSFVDHFKMHQSYLSEHFKSSDGRIGKQSPLLFRLFSELNELLSTTQLPHFLTMINVSAVMEKNSDKQVMDFFNLNNYDCSEGIIKIQRESESVRSQLKEELAEIRKYLKRPYLNFRDEVDYLIEVKNSQIKDLPDDWIKVNNTKMVSRFTTPRTQKLTQKLEYYKDLLIRESELQYKEFLNKITAEYTELRKITLNLAQYDCILSLAATSCNVNYVRPTFVNGQQAIIAKNARNPIIESLDVHYVPNDIMMSPENGKINIITGPNMGGKSSYIRQVALLTIMAQIGSFVPAEEIRLSIFENVLTRIGAHDDIINGDSTFKVEMLDILHILKNCNKRSLLLLDEVGRGTGTHDGIAISYALIKYFSELSDCPLILFTTHFPMLGEIKSPLIRNYHMDYVEEQKTGEDWMSVIFLYKLKKGLTYNSYGMNVAKLARLDKDIINRAFSISEELRKESINEDALKLFSSLKRILKSDNITATDKLAKLLSLDIH
>MSH6_HUMAN__P52701 RecName: Full=DNA mismatch repair protein Msh6; Short=hMSH6; AltName: Full=G/T mismatch-binding protein; Short=GTBP; Short=GTMBP; AltName: Full=MutS-alpha 160 kDa subunit; Short=p160;
MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGASPSPGGDAAWSEAGPGPRPLARSASPPKAKNLNGGLRRSVAPAAPTSCDFSPGDLVWAKMEGYPWWPCLVYNHPFDGTFIREKGKSVRVHVQFFDDSPTRGWVSKRLLKPYTGSKSKEAQKGGHFYSAKPEILRAMQRADEALNKDKIKRLELAVCDEPSEPEEEEEMEVGTTYVTDKSEEDNEIESEEEVQPKTQGSRRSSRQIKKRRVISDSESDIGGSDVEFKPDTKEEGSSDEISSGVGDSESEGLNSPVKVARKRKRMVTGNGSLKRKSSRKETPSATKQATSISSETKNTLRAFSAPQNSESQAHVSGGGDDSSRPTVWYHETLEWLKEEKRRDEHRRRPDHPDFDASTLYVPEDFLNSCTPGMRKWWQIKSQNFDLVICYKVGKFYELYHMDALIGVSELGLVFMKGNWAHSGFPEIAFGRYSDSLVQKGYKVARVEQTETPEMMEARCRKMAHISKYDRVVRREICRIITKGTQTYSVLEGDPSENYSKYLLSLKEKEEDSSGHTRAYGVCFVDTSLGKFFIGQFSDDRHCSRFRTLVAHYPPVQVLFEKGNLSKETKTILKSSLSCSLQEGLIPGSQFWDASKTLRTLLEEEYFREKLSDGIGVMLPQVLKGMTSESDSIGLTPGEKSELALSALGGCVFYLKKCLIDQELLSMANFEEYIPLDSDTVSTTRSGAIFTKAYQRMVLDAVTLNNLEIFLNGTNGSTEGTLLERVDTCHTPFGKRLLKQWLCAPLCNHYAINDRLDAIEDLMVVPDKISEVVELLKKLPDLERLLSKIHNVGSPLKSQNHPDSRAIMYEETTYSKKKIIDFLSALEGFKVMCKIIGIMEEVADGFKSKILKQVISLQTKNPEGRFPDLTVELNRWDTAFDHEKARKTGLITPKAGFDSDYDQALADIRENEQSLLEYLEKQRNRIGCRTIVYWGIGRNRYQLEIPENFTTRNLPEEYELKSTKKGCKRYWTKTIEKKLANLINAEERRDVSLKDCMRRLFYNFDKNYKDWQSAVECIAVLDVLLCLANYSRGGDGPMCRPVILLPEDTPPFLELKGSRHPCITKTFFGDDFIPNDILIGCEEEEQENGKAYCVLVTGPNMGGKSTLMRQAGLLAVMAQMGCYVPAEVCRLTPIDRVFTRLGASDRIMSGESTFFVELSETASILMHATAHSLVLVDELGRGTATFDGTAIANAVVKELAETIKCRTLFSTHYHSLVEDYSQNVAVRLGHMACMVENECEDPSQETITFLYKFIKGACPKSYGFNAARLANLPEEVIQKGHRKAREFEKMNQSLRLFREVCLASERSTVDAEAVHKLLTLIKEL
>MSH6_YEAST__Q03834 RecName: Full=DNA mismatch repair protein MSH6; AltName: Full=MutS protein homolog 6; AltName: Full=Postmeiotic segregation protein 3;
MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKITKNPQGGKTGKLFVDVDEDNDLTIAEETVSTVRSDIMHSQEPQSDTMLNSNTTEPKSTTTDEDLSSSQSRRNHKRRVNYAESDDDDSDTTFTAKRKKGKVVDSESDEDEYLPDKNDGDEDDDIADDKEDIKGELAEDSGDDDDLISLAETTSKKKFSYNTSHSSSPFTRNISRDNSKKKSRPNQAPSRSYNPSHSQPSATSKSSKFNKQNEERYQWLVDERDAQRRPKSDPEYDPRTLYIPSSAWNKFTPFEKQYWEIKSKMWDCIVFFKKGKFFELYEKDALLANALFDLKIAGGGRANMQLAGIPEMSFEYWAAQFIQMGYKVAKVDQRESMLAKEMREGSKGIVKRELQCILTSGTLTDGDMLHSDLATFCLAIREEPGNFYNETQLDSSTIVQKLNTKIFGAAFIDTATGELQMLEFEDDSECTKLDTLMSQVRPMEVVMERNNLSTLANKIVKFNSAPNAIFNEVKAGEEFYDCDKTYAEIISSEYFSTEEDWPEVLKSYYDTGKKVGFSAFGGLLYYLKWLKLDKNLISMKNIKEYDFVKSQHSMVLDGITLQNLEIFSNSFDGSDKGTLFKLFNRAITPMGKRMMKKWLMHPLLRKNDIESRLDSVDSLLQDITLREQLEITFSKLPDLERMLARIHSRTIKVKDFEKVITAFETIIELQDSLKNNDLKGDVSKYISSFPEGLVEAVKSWTNAFERQKAINENIIVPQRGFDIEFDKSMDRIQELEDELMEILMTYRKQFKCSNIQYKDSGKEIYTIEIPISATKNVPSNWVQMAANKTYKRYYSDEVRALARSMAEAKEIHKTLEEDLKNRLCQKFDAHYNTIWMPTIQAISNIDCLLAITRTSEYLGAPSCRPTIVDEVDSKTNTQLNGFLKFKSLRHPCFNLGATTAKDFIPNDIELGKEQPRLGLLTGANAAGKSTILRMACIAVIMAQMGCYVPCESAVLTPIDRIMTRLGANDNIMQGKSTFFVELAETKKILDMATNRSLLVVDELGRGGSSSDGFAIAESVLHHVATHIQSLGFFATHYGTLASSFKHHPQVRPLKMSILVDEATRNVTFLYKMLEGQSEGSFGMHVASMCGISKEIIDNAQIAADNLEHTSRLVKERDLAANNLNGEVVSVPGGLQSDFVRIAYGDGLKNTKLGSGEGVLNYDWNIKRNVLKSLFSIIDDLQS
>RAD2_YEAST__P07276 RecName: Full=DNA repair protein RAD2; EC=3.1.-.-;
MGVHSFWDIAGPTARPVRLESLEDKRMAVDASIWIYQFLKAVRDQEGNAVKNSHITGFFRRICKLLYFGIRPVFVFDGGVPVLKRETIRQRKERRQGKRESAKSTARKLLALQLQNGSNDNVKNSTPSSGSSVQIFKPQDEWDLPDIPGFKYDKEDARVNSNKTFEKLMNSINGDGLEDIDLDTINPASAEFEELPKATQYLILSSLRLKSRLRMGYSKEQLETIFPNSMDFSRFQIDMVKRRNFFTQKLINTTGFQDGGASKLNEEVINRISGQKSKEYKLTKTNNGWILGLGANDGSDAQKAIVIDDKDAGALVKQLDSNAEDGDVLRWDDLEDNSLKIVRHESSNATTAPQKRSNRSEDEGCDSDECEWEEVELKPKNVKFVEDFSLKAARLPYMGQSLNNAGSKSFLDKRHDQASPSKTTPTMRISRISVEDDDEDYLKQIEEIEMMEAVQLSKMEKKPEADDKSKIAKPVTSKGTEARPPIVQYGLLGAQPDSKQPYHVTNLNSKSESVIKRTSKTVLSEFRPPSQQEDKGAILTEGEQNLNFISHKIPQFDFNNENSLLFQKNTESNVSQEATKEKSPIPEMPSWFSSTASQQLYNPYNTTNFVEDKNVRNEQESGAETTNKGSSYELLTGLNATEILERESEKESSNDENKDDDLEVLSEELFEDVPTKSQISKEAEDNDSRKVESINKEHRKPLIFDYDFSEDEEDNIVENMIKEQEEFDTFKNTTLSTSAERNVAENAFVEDELFEQQMKDKRDSDEVTMDMIKEVQELLSRFGIPYITAPMEAEAQCAELLQLNLVDGIITDDSDVFLFGGTKIYKNMFHEKNYVEFYDAESILKLLGLDRKNMIELAQLLGSDYTNGLKGMGPVSSIEVIAEFGNLKNFKDWYNNGQFDKRKQETENKFEKDLRKKLVNNEIILDDDFPSVMVYDAYMRPEVDHDTTPFVWGVPDLDMLRSFMKTQLGWPHEKSDEILIPLIRDVNKRKKKGKQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM
>RFC1_YEAST__P38630 RecName: Full=Replication factor C subunit 1; Short=Replication factor C1; AltName: Full=Activator 1 95 kDa subunit; AltName: Full=Cell division control protein 44;
MVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLDTESDQESTNKTPKKMPVSNVIDVSETPEGEKKLPLPAKRKASSPTVKPASSKKTKPSSKSSDSASNITAQDVLDKIPSLDLSNVHVKENAKFDFKSANSNADPDEIVSEIGSFPEGKPNCLLGLTIVFTGVLPTLERGASEALAKRYGARVTKSISSKTSVVVLGDEAGPKKLEKIKQLKIKAIDEEGFKQLIAGMPAEGGDGEAAEKARRKLEEQHNIATKEAELLVKKEEERSKKLAATRVSGGHLERDNVVREEDKLWTVKYAPTNLQQVCGNKGSVMKLKNWLANWENSKKNSFKHAGKDGSGVFRAAMLYGPPGIGKTTAAHLVAQELGYDILEQNASDVRSKTLLNAGVKNALDNMSVVGYFKHNEEAQNLNGKHFVIIMDEVDGMSGGDRGGVGQLAQFCRKTSTPLILICNERNLPKMRPFDRVCLDIQFRRPDANSIKSRLMTIAIREKFKLDPNVIDRLIQTTRGDIRQVINLLSTISTTTKTINHENINEISKAWEKNIALKPFDIAHKMLDGQIYSDIGSRNFTLNDKIALYFDDFDFTPLMIQENYLSTRPSVLKPGQSHLEAVAEAANCISLGDIVEKKIRSSEQLWSLLPLHAVLSSVYPASKVAGHMAGRINFTAWLGQNSKSAKYYRLLQEIHYHTRLGTSTDKIGLRLDYLPTFRKRLLDPFLKQGADAISSVIEVMDDYYLTKEDWDSIMEFFVGPDVTTAIIKKIPATVKSGFTRKYNSMTHPVAIYRTGSTIGGGGVGTSTSTPDFEDVVDADDNPVPADDEETQDSSTDLKKDKLIKQKAKPTKRKTATSKPGGSKKRKTKA
>RRM3_YEAST__P38766 RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177}; AltName: Full=Regulation of Ty1 transposition protein 104; AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};
MFRSHASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRNITAPPRPRLIRNNSSSLFSQSQGSFGDDDPDAEFKKLVDVPRLNSYKKSSRSLSMTSSLHKTASASTTQKTYHFDEDETLREVTSVKSNSRQLSFTSTINIEDSSMKLSTDSERPAKRSKPSMEFQGLKLTVPKKIKPLLRKTVSNMDSMNHRSASSPVVLTMEQERVVNLIVKKRTNVFYTGSAGTGKSVILQTIIRQLSSLYGKESIAITASTGLAAVTIGGSTLHKWSGIGIGNKTIDQLVKKIQSQKDLLAAWRYTKVLIIDEISMVDGNLLDKLEQIARRIRKNDDPFGGIQLVLTGDFFQLPPVAKKDEHNVVKFCFESEMWKRCIQKTILLTKVFRQQDNKLIDILNAIRYGELTVDIAKTIRNLNRDIDYADGIAPTELYATRREVELSNVKKLQSLPGDLYEFKAVDNAPERYQAILDSSLMVEKVVALKEDAQVMMLKNKPDVELVNGSLGKVLFFVTESLVVKMKEIYKIVDDEVVMDMRLVSRVIGNPLLKESKEFRQDLNARPLARLERLKILINYAVKISPHKEKFPYVRWTVGKNKYIHELMVPERFPIDIPRENVGLERTQIPLMLCWALSIHKAQGQTIQRLKVDLRRIFEAGQVYVALSRAVTMDTLQVLNFDPGKIRTNERVKDFYKRLETLK
>UNG_HUMAN__P13051 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESGDAAAIPAKKAPAGQEEPGTPPSSPLSAEQLDRIQRNKAAALLRLAARNVPVGFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL
>UNG_YEAST__P12887 RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166}; Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166}; EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166}; Flags: Precursor;
MWCMRRLPTNSVMTVARKRKQTTIEDFFGTKKSTNEAPNKKGKSGATFMTITNGAAIKTETKAVAKEANTDKYPANSNAKDVYSKNLSSNLRTLLSLELETIDDSWFPHLMDEFKKPYFVKLKQFVTKEQADHTVFPPAKDIYSWTRLTPFNKVKVVIIGQDPYHNFNQAHGLAFSVKPPTPAPPSLKNIYKELKQEYPDFVEDNKVGDLTHWASQGVLLLNTSLTVRAHNANSHSKHGWETFTKRVVQLLIQDREADGKSLVFLLWGNNAIKLVESLLGSTSVGSGSKYPNIMVMKSVHPSPLSASRGFFGTNHFKMINDWLYNTRGEKMIDWSVVPGTSLREVQEANARLESESKDP
ID   CDN1A_HUMAN             Reviewed;         164 AA.
AC   P38936; Q14010; Q6FI05; Q9BUT4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-NOV-2015, entry version 181.
DE   RecName: Full=Cyclin-dependent kinase inhibitor 1;
DE   AltName: Full=CDK-interacting protein 1;
DE   AltName: Full=Melanoma differentiation-associated protein 6;
DE            Short=MDA-6;
DE   AltName: Full=p21;
GN   Name=CDKN1A; Synonyms=CAP20, CDKN1, CIP1, MDA6, PIC1, SDI1, WAF1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX   PubMed=8242751; DOI=10.1016/0092-8674(93)90499-G;
RA   Harper J.W., Adami G.R., Wei N., Keyomarsi K., Elledge S.J.;
RT   "The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1
RT   cyclin-dependent kinases.";
RL   Cell 75:805-816(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=8242752; DOI=10.1016/0092-8674(93)90500-P;
RA   El-Deiry W.S., Tokino T., Velculescu V.E., Levy D.B., Parsons R.,
RA   Trent J.M., Lin D., Mercer W.E., Kinzler K.W., Vogelstein B.;
RT   "WAF1, a potential mediator of p53 tumor suppression.";
RL   Cell 75:817-825(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8259214; DOI=10.1038/366701a0;
RA   Xiong Y., Hannon G.J., Zhang H., Casso D., Kobayashi R., Beach D.;
RT   "p21 is a universal inhibitor of cyclin kinases.";
RL   Nature 366:701-704(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Jiang H., Fisher P.B.;
RT   "Use of a sensitive and efficient subtraction hybridization protocol
RT   for the identification of genes differentially regulated during the
RT   induction of differentiation in human melanoma cells.";
RL   Mol. Cell. Differ. 1:285-299(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7753561;
RA   Jiang H., Lin J., Su Z.Z., Herlyn M., Kerbel R.S., Weissman B.E.,
RA   Welch D.R., Fisher P.B.;
RT   "The melanoma differentiation-associated gene mda-6, which encodes the
RT   cyclin-dependent kinase inhibitor p21, is differentially expressed
RT   during growth, differentiation and progression in human melanoma
RT   cells.";
RL   Oncogene 10:1855-1864(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8125163; DOI=10.1006/excr.1994.1063;
RA   Noda A., Ning Y., Venable S.F., Pereira-Smith O.M., Smith J.R.;
RT   "Cloning of senescent cell-derived inhibitors of DNA synthesis using
RT   an expression screen.";
RL   Exp. Cell Res. 211:90-98(1994).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-31.
RX   PubMed=7655464; DOI=10.1093/hmg/4.6.1089;
RA   Mousses S., Oezcelik H., Lee P.D., Malkin D., Bull S.B.,
RA   Andrulis I.L.;
RT   "Two variants of the CIP1/WAF1 gene occur together and are associated
RT   with human cancer.";
RL   Hum. Mol. Genet. 4:1089-1092(1995).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-31.
RG   NIEHS SNPs program;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=19054851; DOI=10.1038/nmeth.1273;
RA   Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA   Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA   Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA   Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA   Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA   Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA   Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA   Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA   Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA   Isogai T., Imai J., Watanabe S., Nomura N.;
RT   "Human protein factory for converting the transcriptome into an in
RT   vitro-expressed proteome.";
RL   Nat. Methods 5:1011-1017(2008).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-31.
RC   TISSUE=Eye, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [15]
RP   PROTEIN SEQUENCE OF 2-16, ACETYLATION AT SER-2, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=15574338; DOI=10.1016/j.molcel.2004.11.011;
RA   Chen X., Chi Y., Bloecher A., Aebersold R., Clurman B.E.,
RA   Roberts J.M.;
RT   "N-acetylation and ubiquitin-independent proteasomal degradation of
RT   p21(Cip1).";
RL   Mol. Cell 16:839-847(2004).
RN   [16]
RP   PROTEIN SEQUENCE OF 136-148, PHOSPHORYLATION AT THR-145; SER-146 AND
RP   SER-160, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10753973; DOI=10.1074/jbc.275.15.11529;
RA   Scott M.T., Morrice N., Ball K.L.;
RT   "Reversible phosphorylation at the C-terminal regulatory domain of
RT   p21(Waf1/Cip1) modulates proliferating cell nuclear antigen binding.";
RL   J. Biol. Chem. 275:11529-11537(2000).
RN   [17]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDK4 AND CCND1 IN
RP   THE CYCLIN D-CDK4-CDKN1A COMPLEX.
RX   PubMed=9106657; DOI=10.1101/gad.11.7.847;
RA   LaBaer J., Garrett M.D., Stevenson L.F., Slingerland J.M., Sandhu C.,
RA   Chou H.S., Fattaey A., Harlow E.;
RT   "New functional activities for the p21 family of CDK inhibitors.";
RL   Genes Dev. 11:847-862(1997).
RN   [18]
RP   INTERACTION WITH PSMA3.
RX   PubMed=11350925; DOI=10.1093/emboj/20.10.2367;
RA   Touitou R., Richardson J., Bose S., Nakanishi M., Rivett J.,
RA   Allday M.J.;
RT   "A degradation signal located in the C-terminus of p21WAF1/CIP1 is a
RT   binding site for the C8 alpha-subunit of the 20S proteasome.";
RL   EMBO J. 20:2367-2375(2001).
RN   [19]
RP   PHOSPHORYLATION AT THR-145, MUTAGENESIS OF THR-145 AND SER-146, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=11463845; DOI=10.1128/MCB.21.16.5644-5657.2001;
RA   Roessig L., Jadidi A.S., Urbich C., Badorff C., Zeiher A.M.,
RA   Dimmeler S.;
RT   "Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and
RT   proliferation of endothelial cells.";
RL   Mol. Cell. Biol. 21:5644-5657(2001).
RN   [20]
RP   PHOSPHORYLATION AT THR-145 BY PIM1, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH PIM1.
RX   PubMed=12431783; DOI=10.1016/S0167-4889(02)00347-6;
RA   Wang Z., Bhattacharya N., Mixter P.F., Wei W., Sedivy J.,
RA   Magnuson N.S.;
RT   "Phosphorylation of the cell cycle inhibitor p21Cip1/WAF1 by Pim-1
RT   kinase.";
RL   Biochim. Biophys. Acta 1593:45-55(2002).
RN   [21]
RP   UBIQUITINATION AT SER-2.
RX   PubMed=15226418; DOI=10.1128/MCB.24.14.6140-6150.2004;
RA   Coulombe P., Rodier G., Bonneil E., Thibault P., Meloche S.;
RT   "N-Terminal ubiquitination of extracellular signal-regulated kinase 3
RT   and p21 directs their degradation by the proteasome.";
RL   Mol. Cell. Biol. 24:6140-6150(2004).
RN   [22]
RP   PHOSPHORYLATION AT THR-145.
RX   PubMed=16982699; DOI=10.1128/MCB.00201-06;
RA   Heron-Milhavet L., Franckhauser C., Rana V., Berthenet C., Fisher D.,
RA   Hemmings B.A., Fernandez A., Lamb N.J.;
RT   "Only Akt1 is required for proliferation, while Akt2 promotes cell
RT   cycle exit through p21 binding.";
RL   Mol. Cell. Biol. 26:8267-8280(2006).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [24]
RP   UBIQUITINATION, DOMAIN PIP-BOX K+4 MOTIF, INTERACTION WITH PCNA,
RP   MUTAGENESIS OF SER-114 AND 144-GLN--PHE-150, AND PHOSPHORYLATION AT
RP   SER-114.
RX   PubMed=18794347; DOI=10.1101/gad.1676108;
RA   Abbas T., Sivaprasad U., Terai K., Amador V., Pagano M., Dutta A.;
RT   "PCNA-dependent regulation of p21 ubiquitylation and degradation via
RT   the CRL4Cdt2 ubiquitin ligase complex.";
RL   Genes Dev. 22:2496-2506(2008).
RN   [25]
RP   UBIQUITINATION.
RX   PubMed=18794348; DOI=10.1101/gad.1703708;
RA   Kim Y., Starostina N.G., Kipreos E.T.;
RT   "The CRL4Cdt2 ubiquitin ligase targets the degradation of p21Cip1 to
RT   control replication licensing.";
RL   Genes Dev. 22:2507-2519(2008).
RN   [26]
RP   UBIQUITINATION, DOMAIN PIP-BOX K+4 MOTIF, MUTAGENESIS OF
RP   147-MET--TYR-151 AND 154-LYS--ARG-156, AND INTERACTION WITH PCNA.
RX   PubMed=18703516; DOI=10.1074/jbc.M806045200;
RA   Nishitani H., Shiomi Y., Iida H., Michishita M., Takami T.,
RA   Tsurimoto T.;
RT   "CDK inhibitor p21 is degraded by a proliferating cell nuclear
RT   antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV
RT   irradiation.";
RL   J. Biol. Chem. 283:29045-29052(2008).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [28]
RP   REVIEW ON DNA REPAIR, AND INTERACTION WITH CDK2.
RX   PubMed=19445729; DOI=10.1186/1747-1028-4-9;
RA   Satyanarayana A., Kaldis P.;
RT   "A dual role of Cdk2 in DNA damage response.";
RL   Cell Div. 4:9-9(2009).
RN   [29]
RP   UBIQUITINATION, AND INTERACTION WITH MKRN1.
RX   PubMed=19536131; DOI=10.1038/emboj.2009.164;
RA   Lee E.-W., Lee M.-S., Camus S., Ghim J., Yang M.-R., Oh W., Ha N.-C.,
RA   Lane D.P., Song J.;
RT   "Differential regulation of p53 and p21 by MKRN1 E3 ligase controls
RT   cell cycle arrest and apoptosis.";
RL   EMBO J. 28:2100-2113(2009).
RN   [30]
RP   UBIQUITINATION.
RX   PubMed=19332548; DOI=10.1074/jbc.M808810200;
RA   Stuart S.A., Wang J.Y.;
RT   "Ionizing radiation induces ATM-independent degradation of p21Cip1 in
RT   transformed cells.";
RL   J. Biol. Chem. 284:15061-15070(2009).
RN   [31]
RP   PHOSPHORYLATION AT THR-145 BY PIM2.
RX   PubMed=20307683; DOI=10.1016/j.biocel.2010.03.012;
RA   Wang Z., Zhang Y., Gu J.J., Davitt C., Reeves R., Magnuson N.S.;
RT   "Pim-2 phosphorylation of p21(Cip1/WAF1) enhances its stability and
RT   inhibits cell proliferation in HCT116 cells.";
RL   Int. J. Biochem. Cell Biol. 42:1030-1038(2010).
RN   [32]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [33]
RP   UBIQUITINATION BY RNF114.
RX   PubMed=23645206; DOI=10.1038/cdd.2013.33;
RA   Han J., Kim Y.L., Lee K.W., Her N.G., Ha T.K., Yoon S., Jeong S.I.,
RA   Lee J.H., Kang M.J., Lee M.G., Ryu B.K., Baik J.H., Chi S.G.;
RT   "ZNF313 is a novel cell cycle activator with an E3 ligase activity
RT   inhibiting cellular senescence by destabilizing p21(WAF1.).";
RL   Cell Death Differ. 20:1055-1067(2013).
RN   [34]
RP   FUNCTION, INTERACTION WITH STK11 AND NUAK1, PHOSPHORYLATION AT THR-80
RP   AND SER-146, AND MUTAGENESIS OF THR-80 AND SER-146.
RX   PubMed=25329316; DOI=10.1371/journal.pgen.1004721;
RA   Esteve-Puig R., Gil R., Gonzalez-Sanchez E., Bech-Serra J.J.,
RA   Grueso J., Hernandez-Losa J., Moline T., Canals F., Ferrer B.,
RA   Cortes J., Bastian B., Cajal S.R.Y., Martin-Caballero J., Flores J.M.,
RA   Vivancos A., Garcia-Patos V., Recio J.A.;
RT   "A mouse model uncovers LKB1 as an UVB-induced DNA damage sensor
RT   mediating CDKN1A (p21WAF1/CIP1) degradation.";
RL   PLoS Genet. 10:E1004721-E1004721(2014).
RN   [35]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 139-160 IN COMPLEX WITH PCNA.
RX   PubMed=8861913; DOI=10.1016/S0092-8674(00)81347-1;
RA   Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J.;
RT   "Structure of the C-terminal region of p21(WAF1/CIP1) complexed with
RT   human PCNA.";
RL   Cell 87:297-306(1996).
CC   -!- FUNCTION: May be the important intermediate by which p53/TP53
CC       mediates its role as an inhibitor of cellular proliferation in
CC       response to DNA damage. Binds to and inhibits cyclin-dependent
CC       kinase activity, preventing phosphorylation of critical cyclin-
CC       dependent kinase substrates and blocking cell cycle progression.
CC       Functions in the nuclear localization and assembly of cyclin D-
CC       CDK4 complex and promotes its kinase activity towards RB1. At
CC       higher stoichiometric ratios, inhibits the kinase activity of the
CC       cyclin D-CDK4 complex. {ECO:0000269|PubMed:8242751,
CC       ECO:0000269|PubMed:9106657}.
CC   -!- SUBUNIT: Interacts with HDAC1; the interaction is prevented by
CC       competitive binding of C10orf90/FATS to HDAC1 facilitating
CC       acetylation and protein stabilization of CDKN1A/p21 (By
CC       similarity). Interacts with MKRN1. Interacts with PSMA3. Interacts
CC       with PCNA. Component of the ternary complex, cyclin D-CDK4-CDKN1A.
CC       Interacts (via its N-terminal domain) with CDK4; the interaction
CC       promotes the assembly of the cyclin D-CDK4 complex, its nuclear
CC       translocation and promotes the cyclin D-dependent enzyme activity
CC       of CDK4. Binding to CDK2 leads to CDK2/cyclin E inactivation at
CC       the G1-S phase DNA damage checkpoint, thereby arresting cells at
CC       the G1-S transition during DNA repair. Interacts with PIM1.
CC       Interacts with STK11 and NUAK1. {ECO:0000250|UniProtKB:P39689,
CC       ECO:0000269|PubMed:11350925, ECO:0000269|PubMed:12431783,
CC       ECO:0000269|PubMed:18703516, ECO:0000269|PubMed:18794347,
CC       ECO:0000269|PubMed:19445729, ECO:0000269|PubMed:19536131,
CC       ECO:0000269|PubMed:25329316, ECO:0000269|PubMed:8861913,
CC       ECO:0000269|PubMed:9106657}.
CC   -!- INTERACTION:
CC       P27958:- (xeno); NbExp=3; IntAct=EBI-375077, EBI-6377335;
CC       P78396:CCNA1; NbExp=3; IntAct=EBI-375077, EBI-375065;
CC       P20248:CCNA2; NbExp=2; IntAct=EBI-375077, EBI-457097;
CC       P24385:CCND1; NbExp=11; IntAct=EBI-375077, EBI-375001;
CC       P30279:CCND2; NbExp=6; IntAct=EBI-375077, EBI-748789;
CC       P30281:CCND3; NbExp=10; IntAct=EBI-375077, EBI-375013;
CC       P24864:CCNE1; NbExp=9; IntAct=EBI-375077, EBI-519526;
CC       O96020:CCNE2; NbExp=2; IntAct=EBI-375077, EBI-375033;
CC       O75419:CDC45; NbExp=2; IntAct=EBI-375077, EBI-374969;
CC       Q99741:CDC6; NbExp=2; IntAct=EBI-375077, EBI-374862;
CC       O94921:CDK14; NbExp=8; IntAct=EBI-375077, EBI-1043945;
CC       P24941:CDK2; NbExp=15; IntAct=EBI-375077, EBI-375096;
CC       P11802:CDK4; NbExp=5; IntAct=EBI-375077, EBI-295644;
CC       Q00535:CDK5; NbExp=4; IntAct=EBI-375077, EBI-1041567;
CC       Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-375077, EBI-747204;
CC       Q15323:KRT31; NbExp=3; IntAct=EBI-375077, EBI-948001;
CC       Q9UHC7:MKRN1; NbExp=5; IntAct=EBI-375077, EBI-373524;
CC       Q9BQ15:NABP2; NbExp=7; IntAct=EBI-375077, EBI-2120336;
CC       P12004:PCNA; NbExp=15; IntAct=EBI-375077, EBI-358311;
CC       Q6FI35:PCNA; NbExp=2; IntAct=EBI-375077, EBI-8469539;
CC       Q96FS4:SIPA1; NbExp=2; IntAct=EBI-375077, EBI-1054981;
CC       P63208:SKP1; NbExp=3; IntAct=EBI-375077, EBI-307486;
CC       Q13309:SKP2; NbExp=2; IntAct=EBI-375077, EBI-456291;
CC       P15884:TCF4; NbExp=3; IntAct=EBI-375077, EBI-533224;
CC       Q8IYF3:TEX11; NbExp=4; IntAct=EBI-375077, EBI-742397;
CC       P04637:TP53; NbExp=3; IntAct=EBI-375077, EBI-366083;
CC       Q13077:TRAF1; NbExp=3; IntAct=EBI-375077, EBI-359224;
CC       Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-375077, EBI-2130429;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in all adult tissues, with 5-fold
CC       lower levels observed in the brain.
CC   -!- INDUCTION: Activated by p53/TP53, mezerein (antileukemic compound)
CC       and IFNB1. Repressed by HDAC1. {ECO:0000269|PubMed:8242751,
CC       ECO:0000269|PubMed:8242752}.
CC   -!- DOMAIN: The PIP-box K+4 motif mediates both the interaction with
CC       PCNA and the recuitment of the DCX(DTL) complex: while the PIP-box
CC       interacts with PCNA, the presence of the K+4 submotif, recruits
CC       the DCX(DTL) complex, leading to its ubiquitination.
CC   -!- DOMAIN: The C-terminal is required for nuclear localization of the
CC       cyclin D-CDK4 complex.
CC   -!- PTM: Phosphorylation of Thr-145 by Akt or of Ser-146 by PKC
CC       impairs binding to PCNA. Phosphorylation at Ser-114 by GSK3-beta
CC       enhances ubiquitination by the DCX(DTL) complex. Phosphorylation
CC       of Thr-145 by PIM2 enhances CDKN1A stability and inhibits cell
CC       proliferation. Phosphorylation of Thr-145 by PIM1 results in the
CC       relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein
CC       stability. UV radiation-induced phosphorylation at Thr-80 by LKB1
CC       and at Ser-146 by NUAK1 leads to its degradation.
CC       {ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:11463845,
CC       ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:16982699,
CC       ECO:0000269|PubMed:18794347, ECO:0000269|PubMed:20307683,
CC       ECO:0000269|PubMed:25329316}.
CC   -!- PTM: Ubiquitinated by MKRN1; leading to polyubiquitination and 26S
CC       proteasome-dependent degradation. Ubiquitinated by the DCX(DTL)
CC       complex, also named CRL4(CDT2) complex, leading to its degradation
CC       during S phase or following UV irradiation. Ubiquitination by the
CC       DCX(DTL) complex is essential to control replication licensing and
CC       is PCNA-dependent: interacts with PCNA via its PIP-box, while the
CC       presence of the containing the 'K+4' motif in the PIP box, recruit
CC       the DCX(DTL) complex, leading to its degradation. Ubiquitination
CC       at Ser-2 leads to degradation by the proteasome pathway.
CC       Ubiquitinated by RNF114; leading to proteasomal degradation.
CC       {ECO:0000269|PubMed:15226418}.
CC   -!- PTM: Acetylation leads to protein stability. Acetylated in vitro
CC       on Lys-141, Lys-154, Lys-161 and Lys-163. Deacetylation by HDAC1
CC       is prevented by competitive binding of C10orf90/FATS to HDAC1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CDI family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB59559.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAB59560.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/CDKN1AID139.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/cdkn1a/";
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DR   EMBL; L25610; AAA16109.1; -; mRNA.
DR   EMBL; S67388; AAB29246.1; -; mRNA.
DR   EMBL; U09579; AAA85641.1; -; mRNA.
DR   EMBL; U03106; AAC04313.1; -; mRNA.
DR   EMBL; L26165; AAA19811.1; -; mRNA.
DR   EMBL; L47232; AAB59559.1; ALT_INIT; mRNA.
DR   EMBL; L47233; AAB59560.1; ALT_INIT; mRNA.
DR   EMBL; AF497972; AAM11787.1; -; Genomic_DNA.
DR   EMBL; BT006719; AAP35365.1; -; mRNA.
DR   EMBL; AB451290; BAG70104.1; -; mRNA.
DR   EMBL; AB451422; BAG70236.1; -; mRNA.
DR   EMBL; CR536533; CAG38770.1; -; mRNA.
DR   EMBL; Z85996; CAB06656.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX03904.1; -; Genomic_DNA.
DR   EMBL; BC000275; AAH00275.1; -; mRNA.
DR   EMBL; BC000312; AAH00312.1; -; mRNA.
DR   EMBL; BC001935; AAH01935.1; -; mRNA.
DR   EMBL; BC013967; AAH13967.1; -; mRNA.
DR   CCDS; CCDS4824.1; -.
DR   PIR; I54380; I54380.
DR   PIR; I68674; I68674.
DR   RefSeq; NP_000380.1; NM_000389.4.
DR   RefSeq; NP_001207706.1; NM_001220777.1.
DR   RefSeq; NP_001207707.1; NM_001220778.1.
DR   RefSeq; NP_001278478.1; NM_001291549.1.
DR   RefSeq; NP_510867.1; NM_078467.2.
DR   UniGene; Hs.370771; -.
DR   UniGene; Hs.732576; -.
DR   PDB; 1AXC; X-ray; 2.60 A; B/D/F=139-160.
DR   PDB; 2ZVV; X-ray; 2.00 A; X/Y=139-160.
DR   PDB; 2ZVW; X-ray; 2.50 A; I/J/K/L/M/N/O/P=139-160.
DR   PDB; 4RJF; X-ray; 2.01 A; B/D/F=139-160.
DR   PDBsum; 1AXC; -.
DR   PDBsum; 2ZVV; -.
DR   PDBsum; 2ZVW; -.
DR   PDBsum; 4RJF; -.
DR   DisProt; DP00016; -.
DR   ProteinModelPortal; P38936; -.
DR   SMR; P38936; 17-77.
DR   BioGrid; 107460; 260.
DR   DIP; DIP-246N; -.
DR   IntAct; P38936; 157.
DR   MINT; MINT-104203; -.
DR   STRING; 9606.ENSP00000244741; -.
DR   BindingDB; P38936; -.
DR   ChEMBL; CHEMBL5021; -.
DR   PhosphoSite; P38936; -.
DR   BioMuta; CDKN1A; -.
DR   DMDM; 729143; -.
DR   SWISS-2DPAGE; P38936; -.
DR   PaxDb; P38936; -.
DR   PRIDE; P38936; -.
DR   DNASU; 1026; -.
DR   Ensembl; ENST00000244741; ENSP00000244741; ENSG00000124762.
DR   Ensembl; ENST00000373711; ENSP00000362815; ENSG00000124762.
DR   Ensembl; ENST00000405375; ENSP00000384849; ENSG00000124762.
DR   Ensembl; ENST00000448526; ENSP00000409259; ENSG00000124762.
DR   Ensembl; ENST00000615513; ENSP00000482768; ENSG00000124762.
DR   GeneID; 1026; -.
DR   KEGG; hsa:1026; -.
DR   UCSC; uc003omm.4; human.
DR   CTD; 1026; -.
DR   GeneCards; CDKN1A; -.
DR   HGNC; HGNC:1784; CDKN1A.
DR   HPA; CAB000064; -.
DR   HPA; HPA051359; -.
DR   MIM; 116899; gene.
DR   neXtProt; NX_P38936; -.
DR   Orphanet; 652; Multiple endocrine neoplasia type 1.
DR   PharmGKB; PA104; -.
DR   eggNOG; KOG4743; Eukaryota.
DR   eggNOG; ENOG410XXN5; LUCA.
DR   GeneTree; ENSGT00530000063588; -.
DR   HOGENOM; HOG000285999; -.
DR   HOVERGEN; HBG050868; -.
DR   InParanoid; P38936; -.
DR   KO; K06625; -.
DR   OMA; FAWERVW; -.
DR   OrthoDB; EOG7GJ6HD; -.
DR   PhylomeDB; P38936; -.
DR   TreeFam; TF101038; -.
DR   Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
DR   Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR   Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
DR   Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR   Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR   Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR   Reactome; R-HSA-69563; p53-Dependent G1 DNA Damage Response.
DR   Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   Reactome; R-HSA-69895; Transcriptional activation of cell cycle inhibitor p21.
DR   ChiTaRS; CDKN1A; human.
DR   EvolutionaryTrace; P38936; -.
DR   GeneWiki; P21; -.
DR   GenomeRNAi; 1026; -.
DR   NextBio; 4309; -.
DR   PRO; PR:P38936; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; P38936; -.
DR   CleanEx; HS_CDKN1A; -.
DR   ExpressionAtlas; P38936; baseline and differential.
DR   Genevisible; P38936; HS.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0070557; C:PCNA-p21 complex; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0019912; F:cyclin-dependent protein kinase activating kinase activity; IDA:UniProtKB.
DR   GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; TAS:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:BHF-UCL.
DR   GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:BHF-UCL.
DR   GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; IMP:BHF-UCL.
DR   GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR   GO; GO:0090398; P:cellular senescence; IMP:BHF-UCL.
DR   GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IDA:BHF-UCL.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:BHF-UCL.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:BHF-UCL.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0060574; P:intestinal epithelial cell maturation; IEA:Ensembl.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
DR   GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR   GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0071850; P:mitotic cell cycle arrest; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:BHF-UCL.
DR   GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR   GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IGI:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0042326; P:negative regulation of phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0031100; P:organ regeneration; IEA:Ensembl.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
DR   GO; GO:1904031; P:positive regulation of cyclin-dependent protein kinase activity; IDA:GOC.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:BHF-UCL.
DR   GO; GO:0043068; P:positive regulation of programmed cell death; IEA:Ensembl.
DR   GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
DR   GO; GO:0007265; P:Ras protein signal transduction; IEP:BHF-UCL.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
DR   GO; GO:2000278; P:regulation of DNA biosynthetic process; IEA:Ensembl.
DR   GO; GO:0033158; P:regulation of protein import into nucleus, translocation; IEA:Ensembl.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
DR   GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR   GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR   GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR   GO; GO:0090400; P:stress-induced premature senescence; TAS:BHF-UCL.
DR   InterPro; IPR003175; CDI.
DR   InterPro; IPR029841; CDKN1A_vertebrate.
DR   PANTHER; PTHR10265; PTHR10265; 1.
DR   PANTHER; PTHR10265:SF16; PTHR10265:SF16; 1.
DR   Pfam; PF02234; CDI; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell cycle; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Metal-binding; Nucleus; Phosphoprotein;
KW   Polymorphism; Protein kinase inhibitor; Reference proteome;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:15574338}.
FT   CHAIN         2    164       Cyclin-dependent kinase inhibitor 1.
FT                                /FTId=PRO_0000190079.
FT   ZN_FING      13     41       C4-type. {ECO:0000255}.
FT   REGION       17     24       Required for binding cyclins.
FT   REGION       53     58       Required for binding CDKs.
FT   MOTIF       140    164       PIP-box K+4 motif.
FT   MOTIF       141    156       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000269|PubMed:15574338}.
FT   MOD_RES      80     80       Phosphothreonine; by LKB1.
FT                                {ECO:0000269|PubMed:25329316}.
FT   MOD_RES     114    114       Phosphoserine; by GSK3-beta.
FT                                {ECO:0000269|PubMed:18794347}.
FT   MOD_RES     130    130       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648}.
FT   MOD_RES     145    145       Phosphothreonine; by PKA; PKB/AKT1, PIM1
FT                                and PIM2. {ECO:0000269|PubMed:10753973,
FT                                ECO:0000269|PubMed:11463845,
FT                                ECO:0000269|PubMed:12431783,
FT                                ECO:0000269|PubMed:16982699,
FT                                ECO:0000269|PubMed:20307683}.
FT   MOD_RES     146    146       Phosphoserine; by PKC and NUAK1.
FT                                {ECO:0000269|PubMed:10753973,
FT                                ECO:0000269|PubMed:25329316}.
FT   MOD_RES     160    160       Phosphoserine; by PKC; in vitro.
FT                                {ECO:0000269|PubMed:10753973}.
FT   CROSSLNK      2      2       Glycyl serine ester (Ser-Gly) (interchain
FT                                with G-Cter in ubiquitin).
FT                                {ECO:0000305|PubMed:15226418}.
FT   VARIANT       4      4       P -> L (in dbSNP:rs4986866).
FT                                /FTId=VAR_048686.
FT   VARIANT      31     31       S -> R (in dbSNP:rs1801270).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:7655464,
FT                                ECO:0000269|Ref.8}.
FT                                /FTId=VAR_011870.
FT   VARIANT      63     63       F -> L (in dbSNP:rs4986867).
FT                                /FTId=VAR_048687.
FT   VARIANT     149    149       D -> G (in dbSNP:rs1801724).
FT                                /FTId=VAR_014875.
FT   MUTAGEN      80     80       T->A: Abolishes UV radiation-induced
FT                                phosphorylation and subsequent
FT                                degradation.
FT                                {ECO:0000269|PubMed:25329316}.
FT   MUTAGEN     114    114       S->E: Phosphomimetic mutant, increases
FT                                ubiquitination by the DCX(DTL) complex.
FT                                {ECO:0000269|PubMed:18794347}.
FT   MUTAGEN     144    150       QTSMTDF->ATSATDA: Abolishes interaction
FT                                with PCNA and subsequent degradation by
FT                                the proteasome.
FT                                {ECO:0000269|PubMed:18794347}.
FT   MUTAGEN     145    145       T->A: Reduces phosphorylation by Akt; no
FT                                change in interaction with PCNA, CDK2 or
FT                                CDK4; no change in subcellular location.
FT                                {ECO:0000269|PubMed:11463845}.
FT   MUTAGEN     145    145       T->D: No interaction with PCNA; 59%
FT                                inhibition of CDK2 binding; modest
FT                                inhibition of CDK4 binding; no change in
FT                                subcellular location.
FT                                {ECO:0000269|PubMed:11463845}.
FT   MUTAGEN     146    146       S->A: No change in interaction with PCNA.
FT                                Abolishes UV radiation-induced
FT                                phosphorylation and subsequent
FT                                degradation.
FT                                {ECO:0000269|PubMed:11463845,
FT                                ECO:0000269|PubMed:25329316}.
FT   MUTAGEN     146    146       S->D: Reduces interaction with PCNA.
FT                                {ECO:0000269|PubMed:11463845}.
FT   MUTAGEN     147    151       MTDFY->ATDAAA: Abolishes interaction with
FT                                PCNA and subsequent degradation by the
FT                                proteasome.
FT                                {ECO:0000269|PubMed:18703516}.
FT   MUTAGEN     154    156       KRR->AAA: Abolishes degradation by the
FT                                proteasome without affecting the
FT                                interaction with PCNA.
FT                                {ECO:0000269|PubMed:18703516}.
FT   HELIX       147    149       {ECO:0000244|PDB:2ZVV}.
FT   STRAND      151    158       {ECO:0000244|PDB:4RJF}.
SQ   SEQUENCE   164 AA;  18119 MW;  98D1E7C519ADFCA9 CRC64;
     MSEPAGDVRQ NPCGSKACRR LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLE
     GDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLV
     PRSGEQAEGS PGGPGDSQGR KRRQTSMTDF YHSKRRLIFS KRKP
//
ID   DNLI1_HUMAN             Reviewed;         919 AA.
AC   P18858; B2RAI8; B4DTU4; Q2TB12; Q32P23;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   11-NOV-2015, entry version 174.
DE   RecName: Full=DNA ligase 1;
DE            EC=6.5.1.1;
DE   AltName: Full=DNA ligase I;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
GN   Name=LIG1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=T lymphoblast;
RX   PubMed=2204063; DOI=10.1073/pnas.87.17.6679;
RA   Barnes D.E., Johnston L.H., Kodama K., Tomkinson A.E., Lasko D.D.,
RA   Lindahl T.;
RT   "Human DNA ligase I cDNA: cloning and functional expression in
RT   Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:6679-6683(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-24; TRP-62;
RP   GLU-249; SER-267; MET-349; ILE-369; VAL-480; ILE-614 AND LEU-677.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Placenta, and Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 716-753 (ISOFORM 1).
RX   PubMed=1881902; DOI=10.1073/pnas.88.17.7615;
RA   Petrini J.H.J., Huwiler K.G., Weaver D.T.;
RT   "A wild-type DNA ligase I gene is expressed in Bloom's syndrome
RT   cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:7615-7619(1991).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-76 AND SER-141,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76;
RP   THR-195 AND THR-233, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-76, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA   Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA   Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT   "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT   network: indicating the involvement of ribonucleoside-diphosphate
RT   reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT   Wnt signal transduction.";
RL   Mol. Cell. Proteomics 6:1952-1967(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-141; THR-195;
RP   SER-201; THR-233; SER-911 AND SER-913, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [12]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-422.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18655026; DOI=10.1002/pmic.200700887;
RA   Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,
RA   Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
RT   "Proteomic analysis of ubiquitinated proteins in normal hepatocyte
RT   cell line Chang liver cells.";
RL   Proteomics 8:2885-2896(2008).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51; SER-66;
RP   SER-141; THR-195; SER-201; SER-911 AND SER-913, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-49; SER-51;
RP   SER-66; SER-76; SER-141; THR-195; SER-201 AND SER-911, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76;
RP   SER-141 AND THR-195, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [18]
RP   INTERACTION WITH PCNA.
RX   PubMed=24911150; DOI=10.1172/JCI74593;
RA   Baple E.L., Chambers H., Cross H.E., Fawcett H., Nakazawa Y.,
RA   Chioza B.A., Harlalka G.V., Mansour S., Sreekantan-Nair A.,
RA   Patton M.A., Muggenthaler M., Rich P., Wagner K., Coblentz R.,
RA   Stein C.K., Last J.I., Taylor A.M., Jackson A.P., Ogi T.,
RA   Lehmann A.R., Green C.M., Crosby A.H.;
RT   "Hypomorphic PCNA mutation underlies a human DNA repair disorder.";
RL   J. Clin. Invest. 124:3137-3146(2014).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-919 IN COMPLEX WITH
RP   NICKED DNA AND AMP, COFACTOR, AND ACTIVE SITE.
RX   PubMed=15565146; DOI=10.1038/nature03082;
RA   Pascal J.M., O'Brien P.J., Tomkinson A.E., Ellenberger T.;
RT   "Human DNA ligase I completely encircles and partially unwinds nicked
RT   DNA.";
RL   Nature 432:473-478(2004).
RN   [20]
RP   VARIANTS LYS-566 AND TRP-771.
RX   PubMed=1581963; DOI=10.1016/0092-8674(92)90450-Q;
RA   Barnes D.E., Tomkinson A.E., Lehmann A.R., Webster A.D.B., Lindahl T.;
RT   "Mutations in the DNA ligase I gene of an individual with
RT   immunodeficiencies and cellular hypersensitivity to DNA-damaging
RT   agents.";
RL   Cell 69:495-503(1992).
RN   [21]
RP   VARIANTS [LARGE SCALE ANALYSIS] GLU-152 AND LEU-612.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + diphosphate +
CC       (deoxyribonucleotide)(n+m). {ECO:0000255|PROSITE-
CC       ProRule:PRU10135}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15565146};
CC   -!- SUBUNIT: Interacts with PCNA. {ECO:0000269|PubMed:24911150}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P18858-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P18858-2; Sequence=VSP_056139, VSP_056140;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=P18858-3; Sequence=VSP_057320, VSP_057321;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=LIG1base; Note=LIG1 mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/LIG1base/";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/lig1/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=DNA ligase entry;
CC       URL="https://en.wikipedia.org/wiki/DNA_ligase";
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DR   EMBL; M36067; AAA59518.1; -; mRNA.
DR   EMBL; AF527418; AAM77697.1; -; Genomic_DNA.
DR   EMBL; AK300370; BAG62106.1; -; mRNA.
DR   EMBL; AK314210; BAG36885.1; -; mRNA.
DR   EMBL; AC011466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KC877741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471177; EAW52316.1; -; Genomic_DNA.
DR   EMBL; BC108318; AAI08319.1; -; mRNA.
DR   EMBL; BC110622; AAI10623.1; -; mRNA.
DR   CCDS; CCDS12711.1; -. [P18858-1]
DR   CCDS; CCDS74409.1; -. [P18858-3]
DR   PIR; A36048; A41275.
DR   RefSeq; NP_000225.1; NM_000234.2. [P18858-1]
DR   RefSeq; NP_001275992.1; NM_001289063.1. [P18858-3]
DR   RefSeq; NP_001275993.1; NM_001289064.1.
DR   RefSeq; XP_006723279.1; XM_006723216.2. [P18858-1]
DR   UniGene; Hs.1770; -.
DR   PDB; 1X9N; X-ray; 3.00 A; A=233-919.
DR   PDBsum; 1X9N; -.
DR   ProteinModelPortal; P18858; -.
DR   SMR; P18858; 262-901.
DR   BioGrid; 110166; 6.
DR   DIP; DIP-24215N; -.
DR   IntAct; P18858; 4.
DR   MINT; MINT-141868; -.
DR   STRING; 9606.ENSP00000263274; -.
DR   BindingDB; P18858; -.
DR   ChEMBL; CHEMBL5694; -.
DR   DrugBank; DB00290; Bleomycin.
DR   PhosphoSite; P18858; -.
DR   BioMuta; LIG1; -.
DR   DMDM; 118773; -.
DR   MaxQB; P18858; -.
DR   PaxDb; P18858; -.
DR   PeptideAtlas; P18858; -.
DR   PRIDE; P18858; -.
DR   Ensembl; ENST00000263274; ENSP00000263274; ENSG00000105486. [P18858-1]
DR   Ensembl; ENST00000427526; ENSP00000442841; ENSG00000105486. [P18858-3]
DR   Ensembl; ENST00000601091; ENSP00000471836; ENSG00000105486. [P18858-2]
DR   Ensembl; ENST00000613670; ENSP00000483027; ENSG00000105486. [P18858-2]
DR   GeneID; 3978; -.
DR   KEGG; hsa:3978; -.
DR   UCSC; uc002pia.1; human. [P18858-1]
DR   UCSC; uc010xzg.1; human.
DR   CTD; 3978; -.
DR   GeneCards; LIG1; -.
DR   HGNC; HGNC:6598; LIG1.
DR   HPA; CAB037015; -.
DR   HPA; HPA041431; -.
DR   HPA; HPA048071; -.
DR   MIM; 126391; gene.
DR   neXtProt; NX_P18858; -.
DR   PharmGKB; PA30372; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   GeneTree; ENSGT00810000125528; -.
DR   HOGENOM; HOG000036006; -.
DR   HOVERGEN; HBG005514; -.
DR   InParanoid; P18858; -.
DR   KO; K10747; -.
DR   OMA; PQVVIEV; -.
DR   OrthoDB; EOG7RFTGN; -.
DR   PhylomeDB; P18858; -.
DR   TreeFam; TF300342; -.
DR   BRENDA; 6.5.1.1; 2681.
DR   Reactome; R-HSA-109979; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-HSA-110362; POLB-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-HSA-174414; Processive synthesis on the C-strand of the telomere.
DR   Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-HSA-69183; Processive synthesis on the lagging strand.
DR   Reactome; R-HSA-74969; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR   Reactome; R-HSA-75228; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR   ChiTaRS; LIG1; human.
DR   EvolutionaryTrace; P18858; -.
DR   GeneWiki; LIG1; -.
DR   GenomeRNAi; 3978; -.
DR   NextBio; 15592; -.
DR   PRO; PR:P18858; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; P18858; -.
DR   CleanEx; HS_LIG1; -.
DR   ExpressionAtlas; P18858; baseline and differential.
DR   Genevisible; P18858; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
DR   GO; GO:0003909; F:DNA ligase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR   GO; GO:0006284; P:base-excision repair; IDA:BHF-UCL.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006266; P:DNA ligation; IDA:GOC.
DR   GO; GO:0006259; P:DNA metabolic process; TAS:ProtInc.
DR   GO; GO:0006281; P:DNA repair; TAS:Reactome.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
DR   GO; GO:0006302; P:double-strand break repair; TAS:Reactome.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; TAS:Reactome.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   GO; GO:0006298; P:mismatch repair; TAS:Reactome.
DR   GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0006289; P:nucleotide-excision repair; TAS:Reactome.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
DR   GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IBA:GO_Central.
DR   GO; GO:1903469; P:removal of RNA primer involved in mitotic DNA replication; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0000723; P:telomere maintenance; TAS:Reactome.
DR   GO; GO:0000722; P:telomere maintenance via recombination; TAS:Reactome.
DR   GO; GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Isopeptide bond;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
FT   CHAIN         1    919       DNA ligase 1.
FT                                /FTId=PRO_0000059570.
FT   REGION      449    458       Interaction with target DNA.
FT   REGION      642    644       Interaction with target DNA.
FT   ACT_SITE    568    568       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       621    621       Magnesium 1. {ECO:0000305}.
FT   METAL       720    720       Magnesium 2. {ECO:0000305}.
FT   BINDING     566    566       ATP.
FT   BINDING     573    573       ATP.
FT   BINDING     589    589       ATP.
FT   BINDING     725    725       ATP.
FT   BINDING     738    738       ATP. {ECO:0000250}.
FT   BINDING     744    744       ATP.
FT   SITE        305    305       Interaction with target DNA.
FT   SITE        590    590       Interaction with target DNA.
FT   SITE        770    770       Interaction with target DNA.
FT   SITE        795    795       Interaction with target DNA.
FT   MOD_RES      47     47       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES      49     49       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES      51     51       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES      66     66       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:17693683,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES      76     76       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:17693683,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     141    141       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     195    195       Phosphothreonine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     201    201       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     226    226       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P37913}.
FT   MOD_RES     233    233       Phosphothreonine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648}.
FT   MOD_RES     911    911       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     913    913       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332}.
FT   CROSSLNK    422    422       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:18655026}.
FT   VAR_SEQ       7     36       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_057320.
FT   VAR_SEQ     153    153       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_057321.
FT   VAR_SEQ     796    801       LGTGFS -> VLGNWG (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_056139.
FT   VAR_SEQ     802    919       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_056140.
FT   VARIANT      24     24       A -> V (in dbSNP:rs3730855).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_018802.
FT   VARIANT      52     52       P -> L (in dbSNP:rs4987181).
FT                                /FTId=VAR_020194.
FT   VARIANT      62     62       R -> W (in dbSNP:rs3730863).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_018803.
FT   VARIANT      72     72       D -> G (in dbSNP:rs4987070).
FT                                /FTId=VAR_020195.
FT   VARIANT     152    152       K -> E (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036511.
FT   VARIANT     249    249       G -> E (in dbSNP:rs3730911).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_016766.
FT   VARIANT     267    267       N -> S (in dbSNP:rs3730933).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_016767.
FT   VARIANT     349    349       V -> M (in dbSNP:rs3730947).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_018804.
FT   VARIANT     369    369       V -> I (in dbSNP:rs3730966).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_018805.
FT   VARIANT     409    409       R -> H (in dbSNP:rs4987068).
FT                                /FTId=VAR_016768.
FT   VARIANT     480    480       M -> V (in dbSNP:rs3730980).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_016769.
FT   VARIANT     566    566       E -> K (found in a patient with a
FT                                syndrome of immunodeficiency and
FT                                increased cellular sensitivity to DNA-
FT                                damaging agents due to LIG1 deficiency;
FT                                compound heterozygote carrying W-771).
FT                                {ECO:0000269|PubMed:1581963}.
FT                                /FTId=VAR_002262.
FT   VARIANT     612    612       S -> L (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036512.
FT   VARIANT     614    614       T -> I (in dbSNP:rs3731003).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_016770.
FT   VARIANT     677    677       R -> L (in dbSNP:rs3731008).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_018806.
FT   VARIANT     771    771       R -> W (found in a patient with a
FT                                syndrome of immunodeficiency and
FT                                increased cellular sensitivity to DNA-
FT                                damaging agents due to LIG1 deficiency;
FT                                compound heterozygote carrying K-566).
FT                                {ECO:0000269|PubMed:1581963}.
FT                                /FTId=VAR_002263.
FT   HELIX       263    265       {ECO:0000244|PDB:1X9N}.
FT   HELIX       275    278       {ECO:0000244|PDB:1X9N}.
FT   HELIX       289    300       {ECO:0000244|PDB:1X9N}.
FT   HELIX       305    322       {ECO:0000244|PDB:1X9N}.
FT   HELIX       324    326       {ECO:0000244|PDB:1X9N}.
FT   HELIX       327    335       {ECO:0000244|PDB:1X9N}.
FT   HELIX       341    343       {ECO:0000244|PDB:1X9N}.
FT   HELIX       351    362       {ECO:0000244|PDB:1X9N}.
FT   HELIX       366    376       {ECO:0000244|PDB:1X9N}.
FT   HELIX       379    382       {ECO:0000244|PDB:1X9N}.
FT   HELIX       401    413       {ECO:0000244|PDB:1X9N}.
FT   HELIX       419    433       {ECO:0000244|PDB:1X9N}.
FT   HELIX       438    446       {ECO:0000244|PDB:1X9N}.
FT   HELIX       456    469       {ECO:0000244|PDB:1X9N}.
FT   TURN        483    486       {ECO:0000244|PDB:1X9N}.
FT   HELIX       489    509       {ECO:0000244|PDB:1X9N}.
FT   HELIX       513    527       {ECO:0000244|PDB:1X9N}.
FT   HELIX       529    531       {ECO:0000244|PDB:1X9N}.
FT   STRAND      544    550       {ECO:0000244|PDB:1X9N}.
FT   HELIX       551    557       {ECO:0000244|PDB:1X9N}.
FT   TURN        558    560       {ECO:0000244|PDB:1X9N}.
FT   STRAND      563    578       {ECO:0000244|PDB:1X9N}.
FT   STRAND      584    587       {ECO:0000244|PDB:1X9N}.
FT   TURN        595    597       {ECO:0000244|PDB:1X9N}.
FT   HELIX       599    603       {ECO:0000244|PDB:1X9N}.
FT   HELIX       606    608       {ECO:0000244|PDB:1X9N}.
FT   STRAND      616    625       {ECO:0000244|PDB:1X9N}.
FT   TURN        627    629       {ECO:0000244|PDB:1X9N}.
FT   HELIX       635    638       {ECO:0000244|PDB:1X9N}.
FT   HELIX       648    650       {ECO:0000244|PDB:1X9N}.
FT   STRAND      653    665       {ECO:0000244|PDB:1X9N}.
FT   HELIX       675    685       {ECO:0000244|PDB:1X9N}.
FT   TURN        690    692       {ECO:0000244|PDB:1X9N}.
FT   STRAND      693    695       {ECO:0000244|PDB:1X9N}.
FT   HELIX       704    716       {ECO:0000244|PDB:1X9N}.
FT   STRAND      718    730       {ECO:0000244|PDB:1X9N}.
FT   TURN        735    737       {ECO:0000244|PDB:1X9N}.
FT   STRAND      739    746       {ECO:0000244|PDB:1X9N}.
FT   HELIX       747    751       {ECO:0000244|PDB:1X9N}.
FT   STRAND      755    767       {ECO:0000244|PDB:1X9N}.
FT   STRAND      774    784       {ECO:0000244|PDB:1X9N}.
FT   TURN        785    788       {ECO:0000244|PDB:1X9N}.
FT   STRAND      789    796       {ECO:0000244|PDB:1X9N}.
FT   HELIX       802    814       {ECO:0000244|PDB:1X9N}.
FT   STRAND      816    819       {ECO:0000244|PDB:1X9N}.
FT   STRAND      827    829       {ECO:0000244|PDB:1X9N}.
FT   STRAND      833    836       {ECO:0000244|PDB:1X9N}.
FT   STRAND      841    854       {ECO:0000244|PDB:1X9N}.
FT   TURN        857    861       {ECO:0000244|PDB:1X9N}.
FT   STRAND      867    872       {ECO:0000244|PDB:1X9N}.
FT   STRAND      874    878       {ECO:0000244|PDB:1X9N}.
FT   HELIX       884    886       {ECO:0000244|PDB:1X9N}.
FT   HELIX       890    900       {ECO:0000244|PDB:1X9N}.
SQ   SEQUENCE   919 AA;  101736 MW;  B2854DAE38A8D4AD CRC64;
     MQRSIMSFFH PKKEGKAKKP EKEASNSSRE TEPPPKAALK EWNGVVSESD SPVKRPGRKA
     ARVLGSEGEE EDEALSPAKG QKPALDCSQV SPPRPATSPE NNASLSDTSP MDSSPSGIPK
     RRTARKQLPK RTIQEVLEEQ SEDEDREAKR KKEEEEEETP KESLTEAEVA TEKEGEDGDQ
     PTTPPKPLKT SKAETPTESV SEPEVATKQE LQEEEEQTKP PRRAPKTLSS FFTPRKPAVK
     KEVKEEEPGA PGKEGAAEGP LDPSGYNPAK NNYHPVEDAC WKPGQKVPYL AVARTFEKIE
     EVSARLRMVE TLSNLLRSVV ALSPPDLLPV LYLSLNHLGP PQQGLELGVG DGVLLKAVAQ
     ATGRQLESVR AEAAEKGDVG LVAENSRSTQ RLMLPPPPLT ASGVFSKFRD IARLTGSAST
     AKKIDIIKGL FVACRHSEAR FIARSLSGRL RLGLAEQSVL AALSQAVSLT PPGQEFPPAM
     VDAGKGKTAE ARKTWLEEQG MILKQTFCEV PDLDRIIPVL LEHGLERLPE HCKLSPGIPL
     KPMLAHPTRG ISEVLKRFEE AAFTCEYKYD GQRAQIHALE GGEVKIFSRN QEDNTGKYPD
     IISRIPKIKL PSVTSFILDT EAVAWDREKK QIQPFQVLTT RKRKEVDASE IQVQVCLYAF
     DLIYLNGESL VREPLSRRRQ LLRENFVETE GEFVFATSLD TKDIEQIAEF LEQSVKDSCE
     GLMVKTLDVD ATYEIAKRSH NWLKLKKDYL DGVGDTLDLV VIGAYLGRGK RAGRYGGFLL
     ASYDEDSEEL QAICKLGTGF SDEELEEHHQ SLKALVLPSP RPYVRIDGAV IPDHWLDPSA
     VWEVKCADLS LSPIYPAARG LVDSDKGISL RFPRFIRVRE DKQPEQATTS AQVACLYRKQ
     SQIQNQQGED SGSDPEDTY
//
ID   DNLI1_YEAST             Reviewed;         755 AA.
AC   P04819; D6VRI7; Q12736;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   11-NOV-2015, entry version 170.
DE   RecName: Full=DNA ligase 1;
DE            EC=6.5.1.1;
DE   AltName: Full=DNA ligase I;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
DE   Flags: Precursor;
GN   Name=CDC9; OrderedLocusNames=YDL164C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3909103; DOI=10.1093/nar/13.23.8323;
RA   Barker D.G., White J.H.M., Johnston L.H.;
RT   "The nucleotide sequence of the DNA ligase gene (CDC9) from
RT   Saccharomyces cerevisiae: a gene which is cell-cycle regulated and
RT   induced in response to DNA damage.";
RL   Nucleic Acids Res. 13:8323-8337(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 610-755.
RC   STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
RX   PubMed=8483449;
RA   Wehner E.P., Rao E., Brendel M.;
RT   "Molecular structure and genetic regulation of SFA, a gene responsible
RT   for resistance to formaldehyde in Saccharomyces cerevisiae, and
RT   characterization of its protein product.";
RL   Mol. Gen. Genet. 237:351-358(1993).
RN   [6]
RP   ALTERNATIVE INITIATION.
RX   PubMed=10531002; DOI=10.1016/S0960-9822(99)80477-1;
RA   Willer M., Rainey M., Pullen T., Stirling C.J.;
RT   "The yeast CDC9 gene encodes both a nuclear and a mitochondrial form
RT   of DNA ligase I.";
RL   Curr. Biol. 9:1085-1094(1999).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-75, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-75, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-119 AND SER-123,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM NUCLEAR),
RP   CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM
RP   NUCLEAR), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair. The
CC       mitochondrial form is required for mitochondrial DNA maintenance
CC       but is non-essential while the nuclear form is essential for cell
CC       viability.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + diphosphate +
CC       (deoxyribonucleotide)(n+m). {ECO:0000255|PROSITE-
CC       ProRule:PRU10135}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion.
CC   -!- SUBCELLULAR LOCATION: Isoform Nuclear: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Mitochondrial;
CC         IsoId=P04819-1; Sequence=Displayed;
CC       Name=Nuclear;
CC         IsoId=P04819-2; Sequence=VSP_018719;
CC         Note=Produced by alternative initiation at Met-24 of isoform
CC         Mitochondrial. Initiator Met-1 is removed. Contains a
CC         N-acetylserine at position 2. {ECO:0000244|PubMed:22814378};
CC   -!- MISCELLANEOUS: Cdc9 is included within the category of so-called
CC       'start genes', encoding proteins which are required in early G1,
CC       when the cell is faced with the option of initiating a further
CC       cell cycle.
CC   -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
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DR   EMBL; X03246; CAA27005.1; -; Genomic_DNA.
DR   EMBL; Z67750; CAA91582.1; -; Genomic_DNA.
DR   EMBL; Z74212; CAA98737.1; -; Genomic_DNA.
DR   EMBL; AY723764; AAU09681.1; -; Genomic_DNA.
DR   EMBL; X68020; CAA48158.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11697.1; -; Genomic_DNA.
DR   PIR; S61049; LQBYPX.
DR   RefSeq; NP_010117.1; NM_001180224.1. [P04819-1]
DR   PDB; 2OD8; X-ray; 2.80 A; B=32-53.
DR   PDBsum; 2OD8; -.
DR   ProteinModelPortal; P04819; -.
DR   SMR; P04819; 146-751.
DR   BioGrid; 31901; 50.
DR   DIP; DIP-5630N; -.
DR   IntAct; P04819; 19.
DR   MINT; MINT-499551; -.
DR   MaxQB; P04819; -.
DR   PeptideAtlas; P04819; -.
DR   EnsemblFungi; YDL164C; YDL164C; YDL164C. [P04819-1]
DR   GeneID; 851391; -.
DR   KEGG; sce:YDL164C; -.
DR   EuPathDB; FungiDB:YDL164C; -.
DR   SGD; S000002323; CDC9.
DR   GeneTree; ENSGT00810000125528; -.
DR   HOGENOM; HOG000036006; -.
DR   InParanoid; P04819; -.
DR   KO; K10747; -.
DR   OMA; SQCPNYD; -.
DR   OrthoDB; EOG7TXKRG; -.
DR   BioCyc; YEAST:G3O-29556-MONOMER; -.
DR   Reactome; R-SCE-109979; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-SCE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   Reactome; R-SCE-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   Reactome; R-SCE-75228; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR   EvolutionaryTrace; P04819; -.
DR   NextBio; 968546; -.
DR   PRO; PR:P04819; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005657; C:replication fork; NAS:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IMP:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006266; P:DNA ligation; IDA:SGD.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR   GO; GO:0006273; P:lagging strand elongation; IDA:SGD.
DR   GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:SGD.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:SGD.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative initiation; ATP-binding;
KW   Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transit peptide.
FT   TRANSIT       1     44       Mitochondrion. {ECO:0000255}.
FT   CHAIN        45    755       DNA ligase 1.
FT                                /FTId=PRO_0000007274.
FT   REGION      309    318       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   REGION      493    495       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   ACT_SITE    419    419       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       472    472       Magnesium 1. {ECO:0000250}.
FT   METAL       571    571       Magnesium 2. {ECO:0000250}.
FT   BINDING     417    417       ATP. {ECO:0000250}.
FT   BINDING     424    424       ATP. {ECO:0000250}.
FT   BINDING     440    440       ATP. {ECO:0000250}.
FT   BINDING     576    576       ATP. {ECO:0000250}.
FT   BINDING     590    590       ATP. {ECO:0000250}.
FT   BINDING     596    596       ATP. {ECO:0000250}.
FT   SITE        164    164       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE        441    441       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE        622    622       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE        647    647       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   MOD_RES      58     58       Phosphoserine.
FT                                {ECO:0000244|PubMed:17287358,
FT                                ECO:0000244|PubMed:18407956}.
FT   MOD_RES      75     75       Phosphoserine.
FT                                {ECO:0000244|PubMed:17287358,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES     119    119       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     123    123       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   VAR_SEQ       1     23       Missing (in isoform Nuclear).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_018719.
FT   CONFLICT     69     69       D -> E (in Ref. 1; CAA27005).
FT                                {ECO:0000305}.
FT   CONFLICT    186    186       L -> V (in Ref. 1; CAA27005).
FT                                {ECO:0000305}.
FT   CONFLICT    671    671       G -> E (in Ref. 5; CAA48158).
FT                                {ECO:0000305}.
FT   CONFLICT    724    724       R -> I (in Ref. 5; CAA48158).
FT                                {ECO:0000305}.
FT   HELIX        41     44       {ECO:0000244|PDB:2OD8}.
SQ   SEQUENCE   755 AA;  84828 MW;  B7C2ECAF5C61CAE7 CRC64;
     MRRLLTGCLL SSARPLKSRL PLLMSSSLPS SAGKKPKQAT LARFFTSMKN KPTEGTPSPK
     KSSKHMLEDR MDNVSGEEEY ATKKLKQTAV THTVAAPSSM GSNFSSIPSS APSSGVADSP
     QQSQRLVGEV EDALSSNNND HYSSNIPYSE VCEVFNKIEA ISSRLEIIRI CSDFFIKIMK
     QSSKNLIPTT YLFINRLGPD YEAGLELGLG ENLLMKTISE TCGKSMSQIK LKYKDIGDLG
     EIAMGARNVQ PTMFKPKPLT VGEVFKNLRA IAKTQGKDSQ LKKMKLIKRM LTACKGIEAK
     FLIRSLESKL RIGLAEKTVL ISLSKALLLH DENREDSPDK DVPMDVLESA QQKIRDAFCQ
     VPNYEIVINS CLEHGIMNLD KYCTLRPGIP LKPMLAKPTK AINEVLDRFQ GETFTSEYKY
     DGERAQVHLL NDGTMRIYSR NGENMTERYP EINITDFIQD LDTTKNLILD CEAVAWDKDQ
     GKILPFQVLS TRKRKDVELN DVKVKVCLFA FDILCYNDER LINKSLKERR EYLTKVTKVV
     PGEFQYATQI TTNNLDELQK FLDESVNHSC EGLMVKMLEG PESHYEPSKR SRNWLKLKKD
     YLEGVGDSLD LCVLGAYYGR GKRTGTYGGF LLGCYNQDTG EFETCCKIGT GFSDEMLQLL
     HDRLTPTIID GPKATFVFDS SAEPDVWFEP TTLFEVLTAD LSLSPIYKAG SATFDKGVSL
     RFPRFLRIRE DKGVEDATSS DQIVELYENQ SHMQN
//
ID   DNMT1_HUMAN             Reviewed;        1616 AA.
AC   P26358; A0AV63; B7ZLW6; Q9UHG5; Q9ULA2; Q9UMZ6;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   11-NOV-2015, entry version 180.
DE   RecName: Full=DNA (cytosine-5)-methyltransferase 1;
DE            Short=Dnmt1;
DE            EC=2.1.1.37;
DE   AltName: Full=CXXC-type zinc finger protein 9;
DE   AltName: Full=DNA methyltransferase HsaI;
DE            Short=DNA MTase HsaI;
DE            Short=M.HsaI;
DE   AltName: Full=MCMT;
GN   Name=DNMT1; Synonyms=AIM, CXXC9, DNMT;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1594447; DOI=10.1093/nar/20.9.2287;
RA   Yen R.-W.C., Vertino P.M., Nelkin B.D., Yu J.J., Deiry W.E.,
RA   Cumaraswamy A., Lennon G.G., Trask B.J., Celano P., Baylin S.B.;
RT   "Isolation and characterization of the cDNA encoding human DNA
RT   methyltransferase.";
RL   Nucleic Acids Res. 20:2287-2291(1992).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RX   PubMed=8940105; DOI=10.1074/jbc.271.49.31092;
RA   Yoder J.A., Yen R.-W.C., Vertino P.M., Bestor T.H., Baylin S.B.;
RT   "New 5' regions of the murine and human genes for DNA (cytosine-5)-
RT   methyltransferase.";
RL   J. Biol. Chem. 271:31092-31097(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Prostatic carcinoma;
RA   Li L.C., Au H., Chui R., Dahiya R.;
RT   "Human DNA methyltransferase (DNMT1) is alternatively spliced.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX   PubMed=10449766; DOI=10.1073/pnas.96.17.9751;
RA   Hsu D.-W., Lin M.-J., Lee T.-L., Wen S.-C., Chen X., Shen C.-K.J.;
RT   "Two major forms of DNA (cytosine-5) methyltransferase in human
RT   somatic tissues.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:9751-9756(1999).
RN   [7]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX   PubMed=10753866; DOI=10.1074/jbc.275.15.10754;
RA   Bonfils C., Beaulieu N., Chan E., Cotton-Montpetit J., MacLeod A.R.;
RT   "Characterization of the human DNA methyltransferase splice variant
RT   Dnmt1b.";
RL   J. Biol. Chem. 275:10754-10760(2000).
RN   [8]
RP   INTERACTION WITH PCNA, AND MUTAGENESIS.
RX   PubMed=9302295; DOI=10.1126/science.277.5334.1996;
RA   Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.;
RT   "Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for
RT   p21WAF1.";
RL   Science 277:1996-2000(1997).
RN   [9]
RP   INTERACTION WITH MBD2 AND MBD3.
RX   PubMed=10947852; DOI=10.1046/j.1365-2443.2000.00359.x;
RA   Tatematsu K., Yamazaki T., Ishikawa F.;
RT   "MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex
RT   containing DNMT1 at the replication foci in late S phase.";
RL   Genes Cells 5:677-688(2000).
RN   [10]
RP   INTERACTION WITH HDAC2 AND DMAP1.
RX   PubMed=10888872; DOI=10.1038/77023;
RA   Rountree M.R., Bachman K.E., Baylin S.B.;
RT   "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
RT   replication foci.";
RL   Nat. Genet. 25:269-277(2000).
RN   [11]
RP   INTERACTION WITH RB1; E2F1 AND HDAC1.
RX   PubMed=10888886; DOI=10.1038/77124;
RA   Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L.,
RA   Wolffe A.P.;
RT   "DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses
RT   transcription from E2F-responsive promoters.";
RL   Nat. Genet. 25:338-342(2000).
RN   [12]
RP   TISSUE SPECIFICITY.
RX   PubMed=10325416; DOI=10.1093/nar/27.11.2291;
RA   Robertson K.D., Uzvolgyi E., Liang G., Talmadge C., Sumegi J.,
RA   Gonzales F.A., Jones P.A.;
RT   "The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate
RT   mRNA expression in normal tissues and overexpression in tumors.";
RL   Nucleic Acids Res. 27:2291-2298(1999).
RN   [13]
RP   INTERACTION WITH DNMT3A AND DNMT3B, AND SUBCELLULAR LOCATION.
RX   PubMed=12145218; DOI=10.1093/emboj/cdf401;
RA   Kim G.-D., Ni J., Kelesoglu N., Roberts R.J., Pradhan S.;
RT   "Co-operation and communication between the human maintenance and de
RT   novo DNA (cytosine-5) methyltransferases.";
RL   EMBO J. 21:4183-4195(2002).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-714, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH EED AND EZH2.
RX   PubMed=16357870; DOI=10.1038/nature04431;
RA   Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
RA   Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
RA   Esteller M., Di Croce L., de Launoit Y., Fuks F.;
RT   "The Polycomb group protein EZH2 directly controls DNA methylation.";
RL   Nature 439:871-874(2006).
RN   [16]
RP   ERRATUM.
RA   Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
RA   Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
RA   Esteller M., Di Croce L., de Launoit Y., Fuks F.;
RL   Nature 446:824-824(2006).
RN   [17]
RP   DE NOVO DNA METHYLATION OF TARGET GENES.
RX   PubMed=17200670; DOI=10.1038/ng1950;
RA   Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M.,
RA   Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E.,
RA   Bergman Y., Simon I., Cedar H.;
RT   "Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes
RT   for de novo methylation in cancer.";
RL   Nat. Genet. 39:232-236(2007).
RN   [18]
RP   FUNCTION, AND MUTAGENESIS OF CYS-653; CYS-656; CYS-659; CYS-664;
RP   CYS-667 AND CYS-670.
RX   PubMed=18754681; DOI=10.1021/bi8011725;
RA   Pradhan M., Esteve P.-O., Chin H.G., Samaranayke M., Kim G.-D.,
RA   Pradhan S.;
RT   "CXXC domain of human DNMT1 is essential for enzymatic activity.";
RL   Biochemistry 47:10000-10009(2008).
RN   [19]
RP   FUNCTION.
RX   PubMed=18413740; DOI=10.1158/0008-5472.CAN-07-6654;
RA   Sun L., Huang L., Nguyen P., Bisht K.S., Bar-Sela G., Ho A.S.,
RA   Bradbury C.M., Yu W., Cui H., Lee S., Trepel J.B., Feinberg A.P.,
RA   Gius D.;
RT   "DNA methyltransferase 1 and 3B activate BAG-1 expression via
RT   recruitment of CTCFL/BORIS and modulation of promoter histone
RT   methylation.";
RL   Cancer Res. 68:2726-2735(2008).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [21]
RP   METHYLATION AT LYS-70, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18438403; DOI=10.1038/nchembio.88;
RA   Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,
RA   Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
RT   "Protein lysine methyltransferase G9a acts on non-histone targets.";
RL   Nat. Chem. Biol. 4:344-346(2008).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-143; SER-152;
RP   SER-154 AND SER-394, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [24]
RP   SUMOYLATION, INTERACTION WITH UBC9, AND MUTAGENESIS OF CYS-1226.
RX   PubMed=19450230; DOI=10.1042/BJ20090142;
RA   Lee B., Muller M.T.;
RT   "SUMOylation enhances DNA methyltransferase 1 activity.";
RL   Biochem. J. 421:449-461(2009).
RN   [25]
RP   HOMODIMERIZATION.
RX   PubMed=19173286; DOI=10.1002/jcb.22071;
RA   Fellinger K., Rothbauer U., Felle M., Laengst G., Leonhardt H.;
RT   "Dimerization of DNA methyltransferase 1 is mediated by its regulatory
RT   domain.";
RL   J. Cell. Biochem. 106:521-528(2009).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [27]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173; LYS-1111; LYS-1113 AND
RP   LYS-1115, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-714, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [29]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [30]
RP   PHOSPHORYLATION AT SER-154.
RX   PubMed=21565170; DOI=10.1016/j.bbrc.2011.04.115;
RA   Lavoie G., St-Pierre Y.;
RT   "Phosphorylation of human DNMT1: implication of cyclin-dependent
RT   kinases.";
RL   Biochem. Biophys. Res. Commun. 409:187-192(2011).
RN   [31]
RP   ACETYLATION AT LYS-160; LYS-188; LYS-259; LYS-366; LYS-749; LYS-891;
RP   LYS-957; LYS-961; LYS-975; LYS-1054; LYS-1111; LYS-1113; LYS-1115;
RP   LYS-1117; LYS-1349 AND LYS-1415, AND DEACETYLATION BY SIRT1.
RX   PubMed=21947282; DOI=10.1128/MCB.06147-11;
RA   Peng L., Yuan Z., Ling H., Fukasawa K., Robertson K., Olashaw N.,
RA   Koomen J., Chen J., Lane W.S., Seto E.;
RT   "SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and
RT   alters its activities.";
RL   Mol. Cell. Biol. 31:4720-4734(2011).
RN   [32]
RP   METHYLATION AT LYS-142, AND PHOSPHORYLATION AT SER-143.
RX   PubMed=21151116; DOI=10.1038/nsmb.1939;
RA   Esteve P.O., Chang Y., Samaranayake M., Upadhyay A.K., Horton J.R.,
RA   Feehery G.R., Cheng X., Pradhan S.;
RT   "A methylation and phosphorylation switch between an adjacent lysine
RT   and serine determines human DNMT1 stability.";
RL   Nat. Struct. Mol. Biol. 18:42-48(2011).
RN   [33]
RP   INTERACTION WITH USP7 AND UHRF1.
RX   PubMed=21745816; DOI=10.1093/nar/gkr528;
RA   Felle M., Joppien S., Nemeth A., Diermeier S., Thalhammer V.,
RA   Dobner T., Kremmer E., Kappler R., Langst G.;
RT   "The USP7/Dnmt1 complex stimulates the DNA methylation activity of
RT   Dnmt1 and regulates the stability of UHRF1.";
RL   Nucleic Acids Res. 39:8355-8365(2011).
RN   [34]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-133 AND
RP   SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [35]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 351-600 IN COMPLEX WITH ZINC
RP   IONS.
RX   PubMed=21389349; DOI=10.1074/jbc.M110.209882;
RA   Syeda F., Fagan R.L., Wean M., Avvakumov G.V., Walker J.R., Xue S.,
RA   Dhe-Paganon S., Brenner C.;
RT   "The replication focus targeting sequence (RFTS) domain is a DNA-
RT   competitive inhibitor of Dnmt1.";
RL   J. Biol. Chem. 286:15344-15351(2011).
RN   [37]
RP   X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 646-1600 IN COMPLEX WITH SAH
RP   AND DNA, AND AUTOINHIBITORY LINKER.
RX   PubMed=21163962; DOI=10.1126/science.1195380;
RA   Song J., Rechkoblit O., Bestor T.H., Patel D.J.;
RT   "Structure of DNMT1-DNA complex reveals a role for autoinhibition in
RT   maintenance DNA methylation.";
RL   Science 331:1036-1040(2011).
RN   [38]
RP   VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495, AND CHARACTERIZATION OF
RP   VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495.
RX   PubMed=21532572; DOI=10.1038/ng.830;
RA   Klein C.J., Botuyan M.V., Wu Y., Ward C.J., Nicholson G.A.,
RA   Hammans S., Hojo K., Yamanishi H., Karpf A.R., Wallace D.C., Simon M.,
RA   Lander C., Boardman L.A., Cunningham J.M., Smith G.E., Litchy W.J.,
RA   Boes B., Atkinson E.J., Middha S., Dyck P.J.B., Parisi J.E., Mer G.,
RA   Smith D.I., Dyck P.J.;
RT   "Mutations in DNMT1 cause hereditary sensory neuropathy with dementia
RT   and hearing loss.";
RL   Nat. Genet. 43:595-600(2011).
RN   [39]
RP   VARIANTS ADCADN VAL-554; ALA-589 AND PHE-590.
RX   PubMed=22328086; DOI=10.1093/hmg/dds035;
RA   Winkelmann J., Lin L., Schormair B., Kornum B.R., Faraco J.,
RA   Plazzi G., Melberg A., Cornelio F., Urban A.E., Pizza F., Poli F.,
RA   Grubert F., Wieland T., Graf E., Hallmayer J., Strom T.M., Mignot E.;
RT   "Mutations in DNMT1 cause autosomal dominant cerebellar ataxia,
RT   deafness and narcolepsy.";
RL   Hum. Mol. Genet. 21:2205-2210(2012).
CC   -!- FUNCTION: Methylates CpG residues. Preferentially methylates
CC       hemimethylated DNA. Associates with DNA replication sites in S
CC       phase maintaining the methylation pattern in the newly synthesized
CC       strand, that is essential for epigenetic inheritance. Associates
CC       with chromatin during G2 and M phases to maintain DNA methylation
CC       independently of replication. It is responsible for maintaining
CC       methylation patterns established in development. DNA methylation
CC       is coordinated with methylation of histones. Mediates
CC       transcriptional repression by direct binding to HDAC2. In
CC       association with DNMT3B and via the recruitment of CTCFL/BORIS,
CC       involved in activation of BAG1 gene expression by modulating
CC       dimethylation of promoter histone H3 at H3K4 and H3K9.
CC       {ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:18413740,
CC       ECO:0000269|PubMed:18754681}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
CC       homocysteine + DNA containing 5-methylcytosine.
CC       {ECO:0000255|PROSITE-ProRule:PRU10018}.
CC   -!- SUBUNIT: Binds to CSNK1D (By similarity). Homodimer. Interacts
CC       with HDAC1 and with PCNA. Forms a complex with DMAP1 and HDAC2,
CC       with direct interaction. Forms also a stable complex with E2F1,
CC       BB1 and HDAC1. Binds MBD2 and MBD3. Component of complexes
CC       containing SUV39H1. Interacts with DNMT3A and DNMT3B. Interacts
CC       with the PRC2/EED-EZH2 complex. Interacts with UBC9 and
CC       BAZ2A/TIP5. Interacts with UHRF1; promoting its recruitment to
CC       hemimethylated DNA. Interacts with USP7, promoting its
CC       deubiquitination. {ECO:0000250, ECO:0000269|PubMed:10888872,
CC       ECO:0000269|PubMed:10888886, ECO:0000269|PubMed:10947852,
CC       ECO:0000269|PubMed:12145218, ECO:0000269|PubMed:16357870,
CC       ECO:0000269|PubMed:19450230, ECO:0000269|PubMed:21163962,
CC       ECO:0000269|PubMed:21389349, ECO:0000269|PubMed:21745816,
CC       ECO:0000269|PubMed:9302295}.
CC   -!- INTERACTION:
CC       O75530:EED; NbExp=3; IntAct=EBI-719459, EBI-923794;
CC       Q15910:EZH2; NbExp=8; IntAct=EBI-719459, EBI-530054;
CC       P48552:NRIP1; NbExp=3; IntAct=EBI-719459, EBI-746484;
CC       Q96EB6:SIRT1; NbExp=11; IntAct=EBI-719459, EBI-1802965;
CC       Q96T88:UHRF1; NbExp=12; IntAct=EBI-719459, EBI-1548946;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12145218}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P26358-1; Sequence=Displayed;
CC       Name=2; Synonyms=Dnmt1b;
CC         IsoId=P26358-2; Sequence=VSP_005618;
CC       Name=3;
CC         IsoId=P26358-3; Sequence=VSP_005617;
CC   -!- TISSUE SPECIFICITY: Ubiquitous; highly expressed in fetal tissues,
CC       heart, kidney, placenta, peripheral blood mononuclear cells, and
CC       expressed at lower levels in spleen, lung, brain, small intestine,
CC       colon, liver, and skeletal muscle. Isoform 2 is less expressed
CC       than isoform 1. {ECO:0000269|PubMed:10325416}.
CC   -!- INDUCTION: Its abundance is reduced to non detectable levels at
CC       the G0 phase of the cell cycle and is dramatically induced upon
CC       entrance into the S-phase of the cell cycle.
CC   -!- DOMAIN: The N-terminal part is required for homodimerization and
CC       acts as a regulatory domain.
CC   -!- DOMAIN: The CXXC-type zinc finger specifically binds to
CC       unmethylated CpG dinucleotides, positioning the autoinhibitory
CC       linker between the DNA and the active site, thus providing a
CC       mechanism to ensure that only hemimethylated CpG dinucleotides
CC       undergo methylation. {ECO:0000269|PubMed:21163962}.
CC   -!- PTM: Sumoylated; sumoylation increases activity.
CC       {ECO:0000269|PubMed:19450230}.
CC   -!- PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF,
CC       regulates cell cycle G(2)/M transition. Deacetylation of Lys-1349
CC       and Lys-1415 by SIRT1 increases methyltransferase activity.
CC       {ECO:0000269|PubMed:21947282}.
CC   -!- PTM: Phosphorylation of Ser-154 by CDKs is important for enzymatic
CC       activity and protein stability. Phosphorylation of Ser-143 by AKT1
CC       prevents methylation by SETD7 therebye increasing DNMT1 stability.
CC       {ECO:0000269|PubMed:21151116, ECO:0000269|PubMed:21565170}.
CC   -!- PTM: Methylation at Lys-142 by SETD7 promotes DNMT1 proteasomal
CC       degradation. {ECO:0000269|PubMed:18438403,
CC       ECO:0000269|PubMed:21151116}.
CC   -!- PTM: Ubiquitinated by UHRF1; interaction with USP7 counteracts
CC       ubiquitination by UHRF1 by promoting deubiquitination and
CC       preventing degradation by the proteasome. {ECO:0000250}.
CC   -!- DISEASE: Neuropathy, hereditary sensory, 1E (HSN1E) [MIM:614116]:
CC       A neurodegenerative disorder characterized by adult onset of
CC       progressive peripheral sensory loss associated with progressive
CC       hearing impairment and early-onset dementia.
CC       {ECO:0000269|PubMed:21532572}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Cerebellar ataxia, deafness, and narcolepsy, autosomal
CC       dominant (ADCADN) [MIM:604121]: An autosomal dominant neurologic
CC       disorder characterized by adult onset of progressive cerebellar
CC       ataxia, narcolepsy, cataplexy, sensorineural deafness, and
CC       dementia. More variable features include optic atrophy, sensory
CC       neuropathy, psychosis, and depression.
CC       {ECO:0000269|PubMed:22328086}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. C5-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01016}.
CC   -!- SIMILARITY: Contains 2 BAH domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00370}.
CC   -!- SIMILARITY: Contains 1 CXXC-type zinc finger.
CC       {ECO:0000255|PROSITE-ProRule:PRU00509}.
CC   -!- SIMILARITY: Contains 1 DMAP-interaction domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 SAM-dependent MTase C5-type domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU01016}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD54507.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/DNMT1ID40347ch19p13.html";
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DR   EMBL; X63692; CAA45219.1; -; mRNA.
DR   EMBL; AF180682; AAF23609.1; -; mRNA.
DR   EMBL; AC010077; AAD54507.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC011511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC020931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC126227; AAI26228.1; -; mRNA.
DR   EMBL; BC144093; AAI44094.1; -; mRNA.
DR   EMBL; AH008119; AAD51619.1; -; Genomic_DNA.
DR   CCDS; CCDS12228.1; -. [P26358-1]
DR   CCDS; CCDS45958.1; -. [P26358-2]
DR   PIR; S22610; S22610.
DR   RefSeq; NP_001124295.1; NM_001130823.1. [P26358-2]
DR   RefSeq; NP_001370.1; NM_001379.2. [P26358-1]
DR   UniGene; Hs.202672; -.
DR   PDB; 3EPZ; X-ray; 2.31 A; A/B=351-600.
DR   PDB; 3PTA; X-ray; 3.60 A; A=646-1600.
DR   PDB; 3SWR; X-ray; 2.49 A; A=601-1600.
DR   PDB; 4WXX; X-ray; 2.62 A; A/B=351-1600.
DR   PDB; 4YOC; X-ray; 2.92 A; A=600-1600.
DR   PDBsum; 3EPZ; -.
DR   PDBsum; 3PTA; -.
DR   PDBsum; 3SWR; -.
DR   PDBsum; 4WXX; -.
DR   PDBsum; 4YOC; -.
DR   ProteinModelPortal; P26358; -.
DR   SMR; P26358; 351-599, 601-1600.
DR   BioGrid; 108123; 75.
DR   DIP; DIP-39693N; -.
DR   IntAct; P26358; 22.
DR   MINT; MINT-232346; -.
DR   STRING; 9606.ENSP00000352516; -.
DR   BindingDB; P26358; -.
DR   ChEMBL; CHEMBL1993; -.
DR   DrugBank; DB00928; Azacitidine.
DR   DrugBank; DB01262; Decitabine.
DR   DrugBank; DB01099; Flucytosine.
DR   DrugBank; DB01035; Procainamide.
DR   REBASE; 1161; M.HsaDnmt1A.
DR   PhosphoSite; P26358; -.
DR   BioMuta; DNMT1; -.
DR   DMDM; 12231019; -.
DR   MaxQB; P26358; -.
DR   PaxDb; P26358; -.
DR   PRIDE; P26358; -.
DR   Ensembl; ENST00000340748; ENSP00000345739; ENSG00000130816. [P26358-1]
DR   Ensembl; ENST00000359526; ENSP00000352516; ENSG00000130816. [P26358-2]
DR   Ensembl; ENST00000540357; ENSP00000440457; ENSG00000130816. [P26358-3]
DR   GeneID; 1786; -.
DR   KEGG; hsa:1786; -.
DR   UCSC; uc002mng.3; human. [P26358-1]
DR   UCSC; uc010xlc.2; human. [P26358-2]
DR   CTD; 1786; -.
DR   GeneCards; DNMT1; -.
DR   GeneReviews; DNMT1; -.
DR   HGNC; HGNC:2976; DNMT1.
DR   HPA; CAB005876; -.
DR   HPA; HPA002694; -.
DR   MIM; 126375; gene.
DR   MIM; 604121; phenotype.
DR   MIM; 614116; phenotype.
DR   neXtProt; NX_P26358; -.
DR   Orphanet; 314404; Autosomal dominant cerebellar ataxia, deafness and narcolepsy.
DR   PharmGKB; PA27443; -.
DR   eggNOG; ENOG410IF68; Eukaryota.
DR   eggNOG; COG0270; LUCA.
DR   GeneTree; ENSGT00390000005100; -.
DR   HOGENOM; HOG000082497; -.
DR   HOVERGEN; HBG051384; -.
DR   InParanoid; P26358; -.
DR   KO; K00558; -.
DR   OMA; DEPEMLT; -.
DR   OrthoDB; EOG77WWBH; -.
DR   PhylomeDB; P26358; -.
DR   TreeFam; TF328926; -.
DR   BRENDA; 2.1.1.37; 2681.
DR   Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-HSA-5334118; DNA methylation.
DR   ChiTaRS; DNMT1; human.
DR   EvolutionaryTrace; P26358; -.
DR   GeneWiki; DNMT1; -.
DR   GenomeRNAi; 1786; -.
DR   NextBio; 7267; -.
DR   PRO; PR:P26358; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; P26358; -.
DR   CleanEx; HS_DNMT1; -.
DR   ExpressionAtlas; P26358; baseline and differential.
DR   Genevisible; P26358; HS.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR   GO; GO:0005657; C:replication fork; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0009008; F:DNA-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008327; F:methyl-CpG binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006306; P:DNA methylation; TAS:ProtInc.
DR   GO; GO:0032776; P:DNA methylation on cytosine; TAS:Reactome.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0016458; P:gene silencing; IEA:Ensembl.
DR   GO; GO:0010216; P:maintenance of DNA methylation; IDA:UniProtKB.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
DR   GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; TAS:Reactome.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR   InterPro; IPR010506; DMAP1-bd.
DR   InterPro; IPR017198; DNMT1_meta.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR002857; Znf_CXXC.
DR   Pfam; PF01426; BAH; 2.
DR   Pfam; PF06464; DMAP_binding; 1.
DR   Pfam; PF12047; DNMT1-RFD; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   PIRSF; PIRSF037404; DNMT1; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SMART; SM00439; BAH; 2.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   PROSITE; PS51038; BAH; 2.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative splicing;
KW   Chromatin regulator; Complete proteome; Deafness; Disease mutation;
KW   DNA-binding; Metal-binding; Methylation; Methyltransferase;
KW   Neuropathy; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW   Repeat; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1616       DNA (cytosine-5)-methyltransferase 1.
FT                                /FTId=PRO_0000088034.
FT   DOMAIN       18    103       DMAP-interaction.
FT   DOMAIN      755    880       BAH 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00370}.
FT   DOMAIN      972   1100       BAH 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00370}.
FT   REPEAT     1109   1110       1.
FT   REPEAT     1111   1112       2.
FT   REPEAT     1113   1114       3.
FT   REPEAT     1115   1116       4.
FT   REPEAT     1117   1118       5.
FT   REPEAT     1119   1120       6; approximate.
FT   DOMAIN     1139   1599       SAM-dependent MTase C5-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01016}.
FT   ZN_FING     646    692       CXXC-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00509}.
FT   REGION        1    336       Interaction with the PRC2/EED-EZH2
FT                                complex. {ECO:0000250}.
FT   REGION        1    148       Interaction with DNMT3A.
FT   REGION        1    120       Interaction with DMAP1.
FT   REGION      149    217       Interaction with DNMT3B.
FT   REGION      163    174       Interaction with PCNA.
FT   REGION      308    606       Interaction with the PRC2/EED-EZH2
FT                                complex. {ECO:0000250}.
FT   REGION      310    502       Homodimerization.
FT   REGION      331    550       DNA replication foci-targeting sequence.
FT                                {ECO:0000250}.
FT   REGION      651    697       Required for activity.
FT   REGION      693    754       Autoinhibitory linker.
FT   REGION     1109   1120       6 X 2 AA tandem repeats of K-G.
FT   REGION     1121   1616       Interaction with the PRC2/EED-EZH2
FT                                complex. {ECO:0000250}.
FT   REGION     1139   1616       Catalytic.
FT   MOTIF       177    205       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   ACT_SITE   1226   1226
FT   METAL       353    353       Zinc.
FT   METAL       356    356       Zinc.
FT   METAL       414    414       Zinc.
FT   METAL       418    418       Zinc.
FT   SITE        509    509       Important for activity. {ECO:0000250}.
FT   MOD_RES      70     70       N6,N6-dimethyllysine.
FT                                {ECO:0000269|PubMed:18438403}.
FT   MOD_RES     127    127       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     133    133       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     141    141       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13864}.
FT   MOD_RES     142    142       N6-methyllysine; by SETD7.
FT                                {ECO:0000269|PubMed:21151116}.
FT   MOD_RES     143    143       Phosphoserine; by PKB/AKT1.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000269|PubMed:21151116}.
FT   MOD_RES     152    152       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     154    154       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000269|PubMed:21565170}.
FT   MOD_RES     160    160       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES     173    173       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     188    188       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES     259    259       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES     366    366       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES     394    394       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     509    509       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13864}.
FT   MOD_RES     714    714       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     732    732       Phosphoserine.
FT                                {ECO:0000244|PubMed:18220336}.
FT   MOD_RES     749    749       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES     891    891       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES     957    957       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES     961    961       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES     975    975       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES    1054   1054       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES    1111   1111       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861,
FT                                ECO:0000269|PubMed:21947282}.
FT   MOD_RES    1113   1113       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861,
FT                                ECO:0000269|PubMed:21947282}.
FT   MOD_RES    1115   1115       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861,
FT                                ECO:0000269|PubMed:21947282}.
FT   MOD_RES    1117   1117       N6-acetyllysine; by EHMT2.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES    1119   1119       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P13864}.
FT   MOD_RES    1121   1121       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P13864}.
FT   MOD_RES    1349   1349       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   MOD_RES    1415   1415       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21947282}.
FT   VAR_SEQ       1    336       Missing (in isoform 3).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_005617.
FT   VAR_SEQ     149    149       P -> RSRDPPASASQVTGIRA (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_005618.
FT   VARIANT      97     97       H -> R (in dbSNP:rs16999593).
FT                                /FTId=VAR_024605.
FT   VARIANT     311    311       I -> V (in dbSNP:rs2228612).
FT                                /FTId=VAR_051960.
FT   VARIANT     490    491       DP -> EY (in HSN1E; unstable protein with
FT                                decreased enzymatic activity and impaired
FT                                heterochromatin binding ability after the
FT                                S phase).
FT                                /FTId=VAR_065965.
FT   VARIANT     495    495       Y -> C (in HSN1E; unstable protein with
FT                                decreased enzymatic activity and impaired
FT                                heterochromatin binding ability after the
FT                                S phase). {ECO:0000269|PubMed:21532572}.
FT                                /FTId=VAR_065966.
FT   VARIANT     554    554       A -> V (in ADCADN).
FT                                {ECO:0000269|PubMed:22328086}.
FT                                /FTId=VAR_070055.
FT   VARIANT     589    589       G -> A (in ADCADN).
FT                                {ECO:0000269|PubMed:22328086}.
FT                                /FTId=VAR_070056.
FT   VARIANT     590    590       V -> F (in ADCADN).
FT                                {ECO:0000269|PubMed:22328086}.
FT                                /FTId=VAR_070057.
FT   MUTAGEN     163    163       R->A: Abolishes interaction with PCNA.
FT                                {ECO:0000269|PubMed:9302295}.
FT   MUTAGEN     164    164       Q->A: Abolishes interaction with PCNA.
FT                                {ECO:0000269|PubMed:9302295}.
FT   MUTAGEN     166    166       T->A: Abolishes interaction with PCNA.
FT                                {ECO:0000269|PubMed:9302295}.
FT   MUTAGEN     167    167       I->A: Abolishes interaction with PCNA.
FT                                {ECO:0000269|PubMed:9302295}.
FT   MUTAGEN     169    169       S->A: No loss of interaction with PCNA.
FT                                {ECO:0000269|PubMed:9302295}.
FT   MUTAGEN     170    170       H->V: Abolishes interaction with PCNA.
FT                                {ECO:0000269|PubMed:9302295}.
FT   MUTAGEN     171    171       F->V: Abolishes interaction with PCNA.
FT                                {ECO:0000269|PubMed:9302295}.
FT   MUTAGEN     172    172       A->S: No loss of interaction with PCNA.
FT                                {ECO:0000269|PubMed:9302295}.
FT   MUTAGEN     173    173       K->A: No loss of interaction with PCNA.
FT                                {ECO:0000269|PubMed:9302295}.
FT   MUTAGEN     653    653       C->G: Reduces activity about 10-fold;
FT                                when associated with G-656; G-659; G-664;
FT                                G-667 and G-670.
FT                                {ECO:0000269|PubMed:18754681}.
FT   MUTAGEN     656    656       C->G: Reduces activity about 10-fold;
FT                                when associated with G-653; G-659; G-664;
FT                                G-667 and G-670.
FT                                {ECO:0000269|PubMed:18754681}.
FT   MUTAGEN     659    659       C->G: Reduces activity about 10-fold;
FT                                when associated with G-653; G-656; G-664;
FT                                G-667 and G-670.
FT                                {ECO:0000269|PubMed:18754681}.
FT   MUTAGEN     664    664       C->F: Reduces activity about 10-fold;
FT                                when associated with G-653; G-656; G-659;
FT                                G-667 and G-670.
FT                                {ECO:0000269|PubMed:18754681}.
FT   MUTAGEN     667    667       C->G: Reduces activity about 10-fold;
FT                                when associated with G-653; G-656; G-659;
FT                                G-664 and G-670.
FT                                {ECO:0000269|PubMed:18754681}.
FT   MUTAGEN     670    670       C->G: Reduces activity about 10-fold;
FT                                when associated with G-653; G-656; G-659;
FT                                G-664 and G-667.
FT                                {ECO:0000269|PubMed:18754681}.
FT   MUTAGEN    1226   1226       C->A: Loss of activity.
FT                                {ECO:0000269|PubMed:19450230}.
FT   TURN        354    356       {ECO:0000244|PDB:3EPZ}.
FT   STRAND      359    364       {ECO:0000244|PDB:4WXX}.
FT   HELIX       377    389       {ECO:0000244|PDB:3EPZ}.
FT   STRAND      405    413       {ECO:0000244|PDB:3EPZ}.
FT   STRAND      422    425       {ECO:0000244|PDB:3EPZ}.
FT   TURN        426    430       {ECO:0000244|PDB:3EPZ}.
FT   STRAND      434    441       {ECO:0000244|PDB:3EPZ}.
FT   STRAND      453    458       {ECO:0000244|PDB:3EPZ}.
FT   STRAND      462    467       {ECO:0000244|PDB:3EPZ}.
FT   STRAND      476    480       {ECO:0000244|PDB:3EPZ}.
FT   STRAND      485    488       {ECO:0000244|PDB:3EPZ}.
FT   TURN        493    495       {ECO:0000244|PDB:3EPZ}.
FT   HELIX       496    499       {ECO:0000244|PDB:3EPZ}.
FT   HELIX       504    518       {ECO:0000244|PDB:3EPZ}.
FT   HELIX       524    533       {ECO:0000244|PDB:3EPZ}.
FT   HELIX       538    540       {ECO:0000244|PDB:3EPZ}.
FT   HELIX       547    551       {ECO:0000244|PDB:3EPZ}.
FT   HELIX       554    567       {ECO:0000244|PDB:3EPZ}.
FT   HELIX       575    577       {ECO:0000244|PDB:3EPZ}.
FT   HELIX       579    587       {ECO:0000244|PDB:3EPZ}.
FT   HELIX       592    598       {ECO:0000244|PDB:3EPZ}.
FT   HELIX       622    629       {ECO:0000244|PDB:3SWR}.
FT   TURN        657    659       {ECO:0000244|PDB:3SWR}.
FT   HELIX       670    672       {ECO:0000244|PDB:3SWR}.
FT   TURN        674    677       {ECO:0000244|PDB:4WXX}.
FT   HELIX       687    689       {ECO:0000244|PDB:3SWR}.
FT   HELIX       692    703       {ECO:0000244|PDB:4WXX}.
FT   STRAND      731    735       {ECO:0000244|PDB:3SWR}.
FT   STRAND      738    740       {ECO:0000244|PDB:4WXX}.
FT   STRAND      744    746       {ECO:0000244|PDB:3SWR}.
FT   STRAND      748    752       {ECO:0000244|PDB:3SWR}.
FT   STRAND      755    758       {ECO:0000244|PDB:3SWR}.
FT   STRAND      762    765       {ECO:0000244|PDB:3SWR}.
FT   STRAND      767    769       {ECO:0000244|PDB:3SWR}.
FT   STRAND      775    785       {ECO:0000244|PDB:3SWR}.
FT   TURN        786    788       {ECO:0000244|PDB:3SWR}.
FT   STRAND      789    799       {ECO:0000244|PDB:3SWR}.
FT   HELIX       800    802       {ECO:0000244|PDB:3SWR}.
FT   STRAND      803    805       {ECO:0000244|PDB:4YOC}.
FT   HELIX       806    808       {ECO:0000244|PDB:3SWR}.
FT   STRAND      813    824       {ECO:0000244|PDB:3SWR}.
FT   HELIX       825    827       {ECO:0000244|PDB:3SWR}.
FT   STRAND      828    832       {ECO:0000244|PDB:3SWR}.
FT   STRAND      834    836       {ECO:0000244|PDB:3SWR}.
FT   HELIX       843    845       {ECO:0000244|PDB:3SWR}.
FT   TURN        851    853       {ECO:0000244|PDB:4WXX}.
FT   HELIX       856    860       {ECO:0000244|PDB:3SWR}.
FT   STRAND      862    870       {ECO:0000244|PDB:3SWR}.
FT   TURN        871    874       {ECO:0000244|PDB:3SWR}.
FT   STRAND      875    877       {ECO:0000244|PDB:3SWR}.
FT   STRAND      886    888       {ECO:0000244|PDB:4YOC}.
FT   TURN        889    891       {ECO:0000244|PDB:3SWR}.
FT   HELIX       894    905       {ECO:0000244|PDB:3SWR}.
FT   STRAND      912    916       {ECO:0000244|PDB:3SWR}.
FT   STRAND      921    928       {ECO:0000244|PDB:3SWR}.
FT   STRAND      931    934       {ECO:0000244|PDB:3SWR}.
FT   STRAND      938    941       {ECO:0000244|PDB:3SWR}.
FT   TURN        966    968       {ECO:0000244|PDB:3SWR}.
FT   HELIX       973    975       {ECO:0000244|PDB:3SWR}.
FT   HELIX       976    980       {ECO:0000244|PDB:3SWR}.
FT   STRAND      992   1001       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1005   1008       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1015   1020       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1024   1026       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1031   1034       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1035   1037       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1041   1044       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1048   1052       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1053   1055       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1058   1064       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1065   1067       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1072   1077       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1079   1090       {ECO:0000244|PDB:3SWR}.
FT   TURN       1091   1094       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1095   1097       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1101   1103       {ECO:0000244|PDB:4WXX}.
FT   STRAND     1139   1145       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1150   1158       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1160   1167       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1171   1180       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1184   1187       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1191   1200       {ECO:0000244|PDB:3SWR}.
FT   TURN       1214   1216       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1218   1222       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1231   1233       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1237   1243       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1247   1258       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1261   1268       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1269   1272       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1275   1277       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1278   1289       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1293   1300       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1301   1304       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1311   1318       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1336   1338       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1343   1345       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1348   1350       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1367   1371       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1384   1386       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1395   1401       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1419   1426       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1436   1438       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1451   1453       {ECO:0000244|PDB:3SWR}.
FT   TURN       1462   1464       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1474   1476       {ECO:0000244|PDB:4YOC}.
FT   HELIX      1477   1479       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1480   1482       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1487   1489       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1493   1496       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1499   1503       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1504   1506       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1508   1510       {ECO:0000244|PDB:3SWR}.
FT   TURN       1511   1514       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1523   1525       {ECO:0000244|PDB:3SWR}.
FT   STRAND     1534   1536       {ECO:0000244|PDB:4WXX}.
FT   STRAND     1542   1547       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1550   1556       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1569   1578       {ECO:0000244|PDB:3SWR}.
FT   HELIX      1582   1598       {ECO:0000244|PDB:3SWR}.
SQ   SEQUENCE   1616 AA;  183165 MW;  1E833192D22AFA5B CRC64;
     MPARTAPARV PTLAVPAISL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLQTEIKNQ
     LCDLETKLRK EELSEEGYLA KVKSLLNKDL SLENGAHAYN REVNGRLENG NQARSEARRV
     GMADANSPPK PLSKPRTPRR SKSDGEAKPE PSPSPRITRK STRQTTITSH FAKGPAKRKP
     QEESERAKSD ESIKEEDKDQ DEKRRRVTSR ERVARPLPAE EPERAKSGTR TEKEEERDEK
     EEKRLRSQTK EPTPKQKLKE EPDREARAGV QADEDEDGDE KDEKKHRSQP KDLAAKRRPE
     EKEPEKVNPQ ISDEKDEDEK EEKRRKTTPK EPTEKKMARA KTVMNSKTHP PKCIQCGQYL
     DDPDLKYGQH PPDAVDEPQM LTNEKLSIFD ANESGFESYE ALPQHKLTCF SVYCKHGHLC
     PIDTGLIEKN IELFFSGSAK PIYDDDPSLE GGVNGKNLGP INEWWITGFD GGEKALIGFS
     TSFAEYILMD PSPEYAPIFG LMQEKIYISK IVVEFLQSNS DSTYEDLINK IETTVPPSGL
     NLNRFTEDSL LRHAQFVVEQ VESYDEAGDS DEQPIFLTPC MRDLIKLAGV TLGQRRAQAR
     RQTIRHSTRE KDRGPTKATT TKLVYQIFDT FFAEQIEKDD REDKENAFKR RRCGVCEVCQ
     QPECGKCKAC KDMVKFGGSG RSKQACQERR CPNMAMKEAD DDEEVDDNIP EMPSPKKMHQ
     GKKKKQNKNR ISWVGEAVKT DGKKSYYKKV CIDAETLEVG DCVSVIPDDS SKPLYLARVT
     ALWEDSSNGQ MFHAHWFCAG TDTVLGATSD PLELFLVDEC EDMQLSYIHS KVKVIYKAPS
     ENWAMEGGMD PESLLEGDDG KTYFYQLWYD QDYARFESPP KTQPTEDNKF KFCVSCARLA
     EMRQKEIPRV LEQLEDLDSR VLYYSATKNG ILYRVGDGVY LPPEAFTFNI KLSSPVKRPR
     KEPVDEDLYP EHYRKYSDYI KGSNLDAPEP YRIGRIKEIF CPKKSNGRPN ETDIKIRVNK
     FYRPENTHKS TPASYHADIN LLYWSDEEAV VDFKAVQGRC TVEYGEDLPE CVQVYSMGGP
     NRFYFLEAYN AKSKSFEDPP NHARSPGNKG KGKGKGKGKP KSQACEPSEP EIEIKLPKLR
     TLDVFSGCGG LSEGFHQAGI SDTLWAIEMW DPAAQAFRLN NPGSTVFTED CNILLKLVMA
     GETTNSRGQR LPQKGDVEML CGGPPCQGFS GMNRFNSRTY SKFKNSLVVS FLSYCDYYRP
     RFFLLENVRN FVSFKRSMVL KLTLRCLVRM GYQCTFGVLQ AGQYGVAQTR RRAIILAAAP
     GEKLPLFPEP LHVFAPRACQ LSVVVDDKKF VSNITRLSSG PFRTITVRDT MSDLPEVRNG
     ASALEISYNG EPQSWFQRQL RGAQYQPILR DHICKDMSAL VAARMRHIPL APGSDWRDLP
     NIEVRLSDGT MARKLRYTHH DRKNGRSSSG ALRGVCSCVE AGKACDPAAR QFNTLIPWCL
     PHTGNRHNHW AGLYGRLEWD GFFSTTVTNP EPMGKQGRVL HPEQHRVVSV RECARSQGFP
     DTYRLFGNIL DKHRQVGNAV PPPLAKAIGL EIKLCMLAKA RESASAKIKE EEAAKD
//
ID   DPOD3_HUMAN             Reviewed;         466 AA.
AC   Q15054; B7ZAI6; Q32MZ9; Q32N00;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   11-NOV-2015, entry version 138.
DE   RecName: Full=DNA polymerase delta subunit 3;
DE   AltName: Full=DNA polymerase delta subunit p66;
GN   Name=POLD3; Synonyms=KIAA0039;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Bone marrow;
RX   PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA   Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
RA   Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
RT   "Prediction of the coding sequences of unidentified human genes. I.
RT   The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
RT   analysis of randomly sampled cDNA clones from human immature myeloid
RT   cell line KG-1.";
RL   DNA Res. 1:27-35(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-19 AND 110-123, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RA   Bienvenut W.V., Waridel P., Quadroni M.;
RL   Submitted (MAR-2009) to UniProtKB.
RN   [7]
RP   FUNCTION.
RX   PubMed=10219083; DOI=10.1093/nar/27.10.2108;
RA   Hughes P., Tratner I., Ducoux M., Piard K., Baldacci G.;
RT   "Isolation and identification of the third subunit of mammalian DNA
RT   polymerase delta by PCNA-affinity chromatography of mouse FM3A cell
RT   extracts.";
RL   Nucleic Acids Res. 27:2108-2114(1999).
RN   [8]
RP   FUNCTION.
RX   PubMed=10852724; DOI=10.1021/bi0000871;
RA   Mo J.-Y., Liu L., Leon A., Mazloum N., Lee M.Y.W.T.;
RT   "Evidence that DNA polymerase delta isolated by immunoaffinity
RT   chromatography exhibits high-molecular weight characteristics and is
RT   associated with the KIAA0039 protein and RPA.";
RL   Biochemistry 39:7245-7254(2000).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH PCNA.
RX   PubMed=16510448; DOI=10.1074/jbc.M600322200;
RA   Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y.,
RA   Lee E.Y., Lee M.Y.;
RT   "Functional roles of p12, the fourth subunit of human DNA polymerase
RT   delta.";
RL   J. Biol. Chem. 281:14748-14755(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-407; SER-409;
RP   THR-411; SER-413 AND SER-458, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [19]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-258, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [20]
RP   VARIANTS VAL-194 AND LEU-195.
RX   PubMed=21248752; DOI=10.1038/nature09639;
RA   Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
RA   Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA   Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA   Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA   Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA   Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA   Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA   Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA   Futreal P.A.;
RT   "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT   gene PBRM1 in renal carcinoma.";
RL   Nature 469:539-542(2011).
CC   -!- FUNCTION: Required for optimal DNA polymerase delta activity.
CC       {ECO:0000269|PubMed:10219083, ECO:0000269|PubMed:10852724,
CC       ECO:0000269|PubMed:16510448}.
CC   -!- SUBUNIT: Heterotetramer composed of subunits of 125 kDa, 50 kDa,
CC       66 kDa and 12 kDa. Interacts with POLD2. Interacts with PCNA.
CC       {ECO:0000269|PubMed:16510448}.
CC   -!- INTERACTION:
CC       P12004:PCNA; NbExp=4; IntAct=EBI-864956, EBI-358311;
CC       P49005:POLD2; NbExp=5; IntAct=EBI-864956, EBI-372354;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q15054-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15054-2; Sequence=VSP_054150;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q15054-3; Sequence=VSP_054149;
CC         Note=No experimental confirmation available.;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA05039.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D26018; BAA05039.1; ALT_INIT; mRNA.
DR   EMBL; AK316301; BAH14672.1; -; mRNA.
DR   EMBL; AP001104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW74942.1; -; Genomic_DNA.
DR   EMBL; BC108908; AAI08909.1; -; mRNA.
DR   EMBL; BC108909; AAI08910.1; -; mRNA.
DR   CCDS; CCDS8233.1; -. [Q15054-1]
DR   RefSeq; NP_006582.1; NM_006591.2. [Q15054-1]
DR   UniGene; Hs.82502; -.
DR   PDB; 1U76; X-ray; 2.60 A; B/D/F=452-466.
DR   PDB; 3E0J; X-ray; 3.00 A; B/D/F/H=1-144.
DR   PDBsum; 1U76; -.
DR   PDBsum; 3E0J; -.
DR   ProteinModelPortal; Q15054; -.
DR   SMR; Q15054; 2-144.
DR   BioGrid; 115940; 23.
DR   DIP; DIP-35772N; -.
DR   IntAct; Q15054; 6.
DR   MINT; MINT-2789689; -.
DR   STRING; 9606.ENSP00000263681; -.
DR   PhosphoSite; Q15054; -.
DR   BioMuta; POLD3; -.
DR   DMDM; 17375506; -.
DR   MaxQB; Q15054; -.
DR   PaxDb; Q15054; -.
DR   PeptideAtlas; Q15054; -.
DR   PRIDE; Q15054; -.
DR   Ensembl; ENST00000263681; ENSP00000263681; ENSG00000077514. [Q15054-1]
DR   Ensembl; ENST00000527458; ENSP00000432951; ENSG00000077514. [Q15054-2]
DR   Ensembl; ENST00000532497; ENSP00000436018; ENSG00000077514. [Q15054-3]
DR   GeneID; 10714; -.
DR   KEGG; hsa:10714; -.
DR   UCSC; uc001ovf.2; human. [Q15054-1]
DR   CTD; 10714; -.
DR   GeneCards; POLD3; -.
DR   HGNC; HGNC:20932; POLD3.
DR   HPA; HPA039627; -.
DR   HPA; HPA058846; -.
DR   MIM; 611415; gene.
DR   neXtProt; NX_Q15054; -.
DR   PharmGKB; PA134868595; -.
DR   eggNOG; ENOG410IGGV; Eukaryota.
DR   eggNOG; ENOG410XSD1; LUCA.
DR   GeneTree; ENSGT00390000015282; -.
DR   HOGENOM; HOG000008055; -.
DR   HOVERGEN; HBG051397; -.
DR   InParanoid; Q15054; -.
DR   KO; K03504; -.
DR   OMA; FSAIQCA; -.
DR   PhylomeDB; Q15054; -.
DR   TreeFam; TF103006; -.
DR   Reactome; R-HSA-109977; Repair synthesis for gap-filling by DNA polymerase in TC-NER.
DR   Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR   Reactome; R-HSA-174414; Processive synthesis on the C-strand of the telomere.
DR   Reactome; R-HSA-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR   Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand.
DR   Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-HSA-69091; Polymerase switching.
DR   Reactome; R-HSA-69109; Leading Strand Synthesis.
DR   Reactome; R-HSA-69166; Removal of the Flap Intermediate.
DR   Reactome; R-HSA-69183; Processive synthesis on the lagging strand.
DR   Reactome; R-HSA-74967; Repair synthesis of patch ~27-30 bases long by DNA polymerase.
DR   EvolutionaryTrace; Q15054; -.
DR   GeneWiki; POLD3; -.
DR   GenomeRNAi; 10714; -.
DR   NextBio; 40675; -.
DR   PRO; PR:Q15054; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; Q15054; -.
DR   ExpressionAtlas; Q15054; baseline and differential.
DR   Genevisible; Q15054; HS.
DR   GO; GO:0043625; C:delta DNA polymerase complex; NAS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; NAS:UniProtKB.
DR   GO; GO:0006284; P:base-excision repair; TAS:Reactome.
DR   GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
DR   GO; GO:0006281; P:DNA repair; TAS:Reactome.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
DR   GO; GO:0000731; P:DNA synthesis involved in DNA repair; NAS:UniProtKB.
DR   GO; GO:0006298; P:mismatch repair; NAS:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0006289; P:nucleotide-excision repair; TAS:Reactome.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IMP:UniProtKB.
DR   GO; GO:0000723; P:telomere maintenance; TAS:Reactome.
DR   GO; GO:0000722; P:telomere maintenance via recombination; TAS:Reactome.
DR   GO; GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR   GO; GO:0019985; P:translesion synthesis; TAS:Reactome.
DR   InterPro; IPR019038; DNA_polymerase_subunit_Cdc27.
DR   Pfam; PF09507; CDC27; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   Direct protein sequencing; DNA replication;
KW   DNA-directed DNA polymerase; Isopeptide bond; Nucleotidyltransferase;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW   Transferase; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22223895,
FT                                ECO:0000269|Ref.6}.
FT   CHAIN         2    466       DNA polymerase delta subunit 3.
FT                                /FTId=PRO_0000186047.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:22223895,
FT                                ECO:0000269|Ref.6}.
FT   MOD_RES     307    307       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     407    407       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     409    409       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     411    411       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     413    413       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     458    458       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   CROSSLNK    258    258       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   VAR_SEQ       1    106       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_054149.
FT   VAR_SEQ       1     39       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_054150.
FT   VARIANT     194    194       G -> V (found in a renal cell carcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:21248752}.
FT                                /FTId=VAR_064745.
FT   VARIANT     195    195       M -> L (found in a renal cell carcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:21248752}.
FT                                /FTId=VAR_064746.
FT   HELIX         3     14       {ECO:0000244|PDB:3E0J}.
FT   TURN         15     17       {ECO:0000244|PDB:3E0J}.
FT   HELIX        23     30       {ECO:0000244|PDB:3E0J}.
FT   HELIX        34     52       {ECO:0000244|PDB:3E0J}.
FT   STRAND       58     81       {ECO:0000244|PDB:3E0J}.
FT   TURN         82     84       {ECO:0000244|PDB:3E0J}.
FT   HELIX        85     91       {ECO:0000244|PDB:3E0J}.
FT   STRAND       93    106       {ECO:0000244|PDB:3E0J}.
FT   STRAND      109    111       {ECO:0000244|PDB:3E0J}.
FT   HELIX       113    125       {ECO:0000244|PDB:3E0J}.
FT   HELIX       129    131       {ECO:0000244|PDB:3E0J}.
FT   STRAND      134    136       {ECO:0000244|PDB:3E0J}.
FT   HELIX       459    461       {ECO:0000244|PDB:1U76}.
SQ   SEQUENCE   466 AA;  51400 MW;  E9625E0188725F45 CRC64;
     MADQLYLENI DEFVTDQNKI VTYKWLSYTL GVHVNQAKQM LYDYVERKRK ENSGAQLHVT
     YLVSGSLIQN GHSCHKVAVV REDKLEAVKS KLAVTASIHV YSIQKAMLKD SGPLFNTDYD
     ILKSNLQNCS KFSAIQCAAA VPRAPAESSS SSKKFEQSHL HMSSETQANN ELTTNGHGPP
     ASKQVSQQPK GIMGMFASKA AAKTQETNKE TKTEAKEVTN ASAAGNKAPG KGNMMSNFFG
     KAAMNKFKVN LDSEQAVKEE KIVEQPTVSV TEPKLATPAG LKKSSKKAEP VKVLQKEKKR
     GKRVALSDDE TKETENMRKK RRRIKLPESD SSEDEVFPDS PGAYEAESPS PPPPPSPPLE
     PVPKTEPEPP SVKSSSGENK RKRKRVLKSK TYLDGEGCIV TEKVYESESC TDSEEELNMK
     TSSVHRPPAM TVKKEPREER KGPKKGTAAL GKANRQVSIT GFFQRK
//
ID   DPOD3_YEAST             Reviewed;         350 AA.
AC   P47110; D6VWL4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   11-NOV-2015, entry version 126.
DE   RecName: Full=DNA polymerase delta subunit 3;
GN   Name=POL32; OrderedLocusNames=YJR043C; ORFNames=J1626;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7668047; DOI=10.1002/yea.320110809;
RA   Huang M.-E., Chuat J.-C., Galibert F.;
RT   "Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA
RT   genes and 14 new open reading frames including a gene most probably
RT   belonging to the family of ubiquitin-protein ligases.";
RL   Yeast 11:775-781(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
RA   Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
RA   Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
RA   Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
RA   Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
RA   Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
RA   Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
RA   Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
RA   Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
RA   Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
RA   Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=9677405; DOI=10.1074/jbc.273.31.19747;
RA   Gerik K.J., Li X., Pautz A., Burgers P.M.;
RT   "Characterization of the two small subunits of Saccharomyces
RT   cerevisiae DNA polymerase delta.";
RL   J. Biol. Chem. 273:19747-19755(1998).
RN   [6]
RP   COMPOSITION OF THE DNA POLYMERASE DELTA COMPLEX.
RX   PubMed=11568188; DOI=10.1074/jbc.M108842200;
RA   Johansson E., Majka J., Burgers P.M.;
RT   "Structure of DNA polymerase delta from Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 276:43824-43828(2001).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223 AND SER-230, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: DNA polymerase delta (DNA polymerase III) participates
CC       in chromosomal DNA replication. It is required during synthesis of
CC       the leading and lagging DNA strands at the replication fork and
CC       binds at/or near replication origins and moves along DNA with the
CC       replication fork. It has 3'-5' proofreading exonuclease activity
CC       that correct errors arising during DNA replication. It is also
CC       involved in DNA synthesis during DNA repair.
CC   -!- SUBUNIT: DNA polymerase delta is a heterotrimer of POL3, POL32 and
CC       HYS2. POL32 can form homodimers.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 2410 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; L36344; AAA88745.1; -; Genomic_DNA.
DR   EMBL; Z49543; CAA89571.1; -; Genomic_DNA.
DR   EMBL; AY557918; AAS56244.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08830.1; -; Genomic_DNA.
DR   PIR; S57062; S57062.
DR   RefSeq; NP_012577.1; NM_001181701.1.
DR   ProteinModelPortal; P47110; -.
DR   BioGrid; 33794; 282.
DR   DIP; DIP-2523N; -.
DR   IntAct; P47110; 9.
DR   MINT; MINT-477170; -.
DR   MaxQB; P47110; -.
DR   PRIDE; P47110; -.
DR   EnsemblFungi; YJR043C; YJR043C; YJR043C.
DR   GeneID; 853500; -.
DR   KEGG; sce:YJR043C; -.
DR   EuPathDB; FungiDB:YJR043C; -.
DR   SGD; S000003804; POL32.
DR   HOGENOM; HOG000112262; -.
DR   InParanoid; P47110; -.
DR   KO; K03504; -.
DR   OMA; DCFIYAF; -.
DR   OrthoDB; EOG7R5765; -.
DR   BioCyc; YEAST:G3O-31678-MONOMER; -.
DR   NextBio; 974143; -.
DR   PRO; PR:P47110; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   GO; GO:0043625; C:delta DNA polymerase complex; TAS:SGD.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:SGD.
DR   GO; GO:0006284; P:base-excision repair; TAS:SGD.
DR   GO; GO:0006277; P:DNA amplification; IMP:SGD.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IDA:SGD.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR   GO; GO:0006273; P:lagging strand elongation; TAS:SGD.
DR   GO; GO:0006272; P:leading strand elongation; TAS:SGD.
DR   GO; GO:0006298; P:mismatch repair; NAS:SGD.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; TAS:GOC.
DR   GO; GO:0006289; P:nucleotide-excision repair; TAS:SGD.
DR   GO; GO:0006301; P:postreplication repair; TAS:SGD.
DR   GO; GO:0006278; P:RNA-dependent DNA replication; IDA:SGD.
PE   1: Evidence at protein level;
KW   Complete proteome; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN         1    350       DNA polymerase delta subunit 3.
FT                                /FTId=PRO_0000186050.
FT   MOD_RES     223    223       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     230    230       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
SQ   SEQUENCE   350 AA;  40310 MW;  D0B9CC52F26E20B2 CRC64;
     MDQKASYFIN EKLFTEVKPV LFTDLIHHLK IGPSMAKKLM FDYYKQTTNA KYNCVVICCY
     KDQTIKIIHD LSNIPQQDSI IDCFIYAFNP MDSFIPYYDI IDQKDCLTIK NSYELKVSES
     SKIIERTKTL EEKSKPLVRP TARSKTTPEE TTGRKSKSKD MGLRSTALLA KMKKDRDDKE
     TSRQNELRKR KEENLQKINK QNPEREAQMK ELNNLFVEDD LDTEEVNGGS KPNSPKETDS
     NDKDKNNDDL EDLLETTAED SLMDVPKIQQ TKPSETEHSK EPKSEEEPSS FIDEDGYIVT
     KRPATSTPPR KPSPVVKRAL SSSKKQETPS SNKRLKKQGT LESFFKRKAK
//
ID   DPOD3_SCHPO             Reviewed;         372 AA.
AC   P30261;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   11-NOV-2015, entry version 102.
DE   RecName: Full=DNA polymerase delta subunit 3;
DE   AltName: Full=Cell division control protein 27;
GN   Name=cdc27; ORFNames=SPBC1734.02c, SPBC337.18c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=1538696; DOI=10.1007/BF00292709;
RA   Hughes D.A., Macneill S.A., Fantes P.A.;
RT   "Molecular cloning and sequence analysis of cdc27+ required for the
RT   G2-M transition in the fission yeast Schizosaccharomyces pombe.";
RL   Mol. Gen. Genet. 231:401-410(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=10671561; DOI=10.1074/jbc.275.7.5153;
RA   Zuo S., Bermudez V., Zhang G., Kelman Z., Hurwitz J.;
RT   "Structure and activity associated with multiple forms of
RT   Schizosaccharomyces pombe DNA polymerase delta.";
RL   J. Biol. Chem. 275:5153-5162(2000).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- SUBUNIT: Heterotetramer that consist of the pol3, cdc1, cdc27 and
CC       cdm1 subunits. Cdc27 interacts with cdc1 and is required for
CC       dimerization of the tetramer. {ECO:0000269|PubMed:10671561}.
CC   -!- INTERACTION:
CC       P87324:cdc1; NbExp=3; IntAct=EBI-866919, EBI-865227;
CC       Q03392:pcn1; NbExp=5; IntAct=EBI-866919, EBI-768724;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M74062; AAA35295.1; -; Genomic_DNA.
DR   EMBL; M83307; AAA35296.1; -; mRNA.
DR   EMBL; CU329671; CAA21288.1; -; Genomic_DNA.
DR   PIR; T39649; T39649.
DR   RefSeq; NP_595419.1; NM_001021326.2.
DR   BioGrid; 276184; 20.
DR   IntAct; P30261; 2.
DR   MINT; MINT-4688159; -.
DR   MaxQB; P30261; -.
DR   EnsemblFungi; SPBC1734.02c.1; SPBC1734.02c.1:pep; SPBC1734.02c.
DR   GeneID; 2539627; -.
DR   KEGG; spo:SPBC1734.02c; -.
DR   EuPathDB; FungiDB:SPBC1734.02c; -.
DR   PomBase; SPBC1734.02c; cdc27.
DR   InParanoid; P30261; -.
DR   KO; K03504; -.
DR   OrthoDB; EOG7XPZFV; -.
DR   NextBio; 20800783; -.
DR   PRO; PR:P30261; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0043625; C:delta DNA polymerase complex; IDA:PomBase.
DR   GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IDA:PomBase.
DR   GO; GO:1904161; P:DNA synthesis involved in UV-damage excision repair; IDA:PomBase.
DR   GO; GO:1903459; P:mitotic DNA replication lagging strand elongation; IC:PomBase.
DR   GO; GO:0007067; P:mitotic nuclear division; IEA:UniProtKB-KW.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IC:GOC.
DR   InterPro; IPR019038; DNA_polymerase_subunit_Cdc27.
DR   Pfam; PF09507; CDC27; 2.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Complete proteome; DNA replication;
KW   DNA-directed DNA polymerase; Mitosis; Nucleotidyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN         1    372       DNA polymerase delta subunit 3.
FT                                /FTId=PRO_0000186049.
FT   MOD_RES     163    163       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MUTAGEN      57     57       G->E: Cell cycle arrest at 35 degrees
FT                                Celsius.
FT   MUTAGEN      57     57       G->R: Cell cycle arrest at 35 degrees
FT                                Celsius.
SQ   SEQUENCE   372 AA;  42350 MW;  6E6F9AD407B17673 CRC64;
     MEEWRNFLDI KVINESSLVT VDNLSLQLDI SSEKAQEYLN MFYQGNDFLY PIYLIHGQPI
     DDEINLEIDE ESQPISNFPV LQYILCDKSS LQEKQSRLKS GYKTVIFALS SAPLSDFDEL
     LPAVYEIREK DVLYKKEDAD KYGFIFNENS VPRVLKKAPS THSPQLSVPS KTSTIDKTDT
     RSTEKTKGKD IFSNARNQKG NSSRKNKKAP LENHKEKEPL LPKEEKLSEQ AKRERDDLKN
     IMQLEDESVS TTSVHDSEDD NLDSNNFQLE IGTEAKSAAP DEPQEIIKSV SGGKRRGKRK
     VKKYATTKDE EGFLVTKEEE VWESFSEDEN ISTGTSNVVR NKPTTVNIAT KKKNTAQSKP
     QQKSIMSFFG KK
//
ID   ERCC5_HUMAN             Reviewed;        1186 AA.
AC   P28715; A6NGT4; Q5JUS4; Q5JUS5; Q7Z2V3; Q8IZL6; Q8N1B7; Q9HD59;
AC   Q9HD60;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 3.
DT   11-NOV-2015, entry version 185.
DE   RecName: Full=DNA repair protein complementing XP-G cells;
DE            EC=3.1.-.-;
DE   AltName: Full=DNA excision repair protein ERCC-5;
DE   AltName: Full=Xeroderma pigmentosum group G-complementing protein;
GN   Name=ERCC5; Synonyms=ERCM2, XPG, XPGC;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-1053;
RP   ARG-1080 AND HIS-1104.
RX   PubMed=8483504; DOI=10.1038/363182a0;
RA   Scherly D., Nouspikel T., Corlet J., Ucla C., Bairoch A.,
RA   Clarkson S.G.;
RT   "Complementation of the DNA repair defect in Xeroderma pigmentosum
RT   group G cells by a human cDNA related to yeast RAD2.";
RL   Nature 363:182-185(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS VAL-254; ARG-1053
RP   AND ARG-1080.
RX   PubMed=7510366; DOI=10.1016/0921-8777(94)90080-9;
RA   Shiomi T., Harada Y.-N., Saito T., Shiomi N., Okuno Y., Yamaizumi M.;
RT   "An ERCC5 gene with homology to yeast RAD2 is involved in group G
RT   Xeroderma pigmentosum.";
RL   Mutat. Res. 314:167-175(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS VAL-254; ARG-1053
RP   AND ARG-1080.
RX   PubMed=8413238;
RA   Macinnes M.A., Dickson J.A., Hernandez R.R., Learmonth D., Lin G.Y.,
RA   Mudgett J.S., Park M.S., Schauer S., Reynolds R.J., Strniste G.F.,
RA   Yu J.Y.;
RT   "Human ERCC5 cDNA-cosmid complementation for excision repair and
RT   bipartite amino acid domains conserved with RAD proteins of
RT   Saccharomyces cerevisiae and Schizosaccharomyces pombe.";
RL   Mol. Cell. Biol. 13:6393-6402(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
RP   1 AND 3).
RX   PubMed=11266544; DOI=10.1093/nar/29.7.1443;
RA   Emmert S., Schneider T.D., Khan S.G., Kraemer K.H.;
RT   "The human XPG gene: gene architecture, alternative splicing and
RT   single nucleotide polymorphisms.";
RL   Nucleic Acids Res. 29:1443-1452(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP   VAL-254; ARG-1053 AND ARG-1080.
RC   TISSUE=Bone marrow;
RA   Zan Q., Guo J.H., Yu L.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-181; VAL-254;
RP   ARG-256; CYS-311; LYS-399; SER-529; ILE-590; LEU-597; SER-879;
RP   HIS-1009 AND ARG-1053; ARG-1080 AND GLN-1080.
RG   NIEHS SNPs program;
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA   Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA   Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA   Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA   Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA   Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA   Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA   Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA   Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA   Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA   Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA   Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA   King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA   Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA   Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA   Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA   Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA   Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA   Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP   ARG-1053 AND ARG-1080.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
RX   PubMed=8088806; DOI=10.1006/geno.1994.1261;
RA   Samec S., Jones T.A., Corlet J., Scherly D., Sheer D., Wood R.D.,
RA   Clarkson S.G.;
RT   "The human gene for Xeroderma pigmentosum complementation group G
RT   (XPG) maps to 13q33 by fluorescence in situ hybridization.";
RL   Genomics 21:283-285(1994).
RN   [10]
RP   CHARACTERIZATION.
RX   PubMed=8206890;
RA   O'Donovan A., Scherly D., Clarkson S.G., Wood R.D.;
RT   "Isolation of active recombinant XPG protein, a human DNA repair
RT   endonuclease.";
RL   J. Biol. Chem. 269:15965-15968(1994).
RN   [11]
RP   CHARACTERIZATION.
RX   PubMed=8090225; DOI=10.1038/371432a0;
RA   O'Donovan A., Davies A.A., Moggs J.G., West S.C., Wood R.D.;
RT   "XPG endonuclease makes the 3' incision in human DNA nucleotide
RT   excision repair.";
RL   Nature 371:432-435(1994).
RN   [12]
RP   CHARACTERIZATION.
RX   PubMed=8078765; DOI=10.1093/nar/22.16.3312;
RA   Habraken Y., Sung P., Prakash L., Prakash S.;
RT   "Human Xeroderma pigmentosum group G gene encodes a DNA
RT   endonuclease.";
RL   Nucleic Acids Res. 22:3312-3316(1994).
RN   [13]
RP   CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX   PubMed=7651464; DOI=10.1016/0165-7992(95)90070-5;
RA   Cloud K.G., Shen B., Strniste G.F., Park M.S.;
RT   "XPG protein has a structure-specific endonuclease activity.";
RL   Mutat. Res. 347:55-60(1995).
RN   [14]
RP   INTERACTION WITH PCNA.
RX   PubMed=9305916; DOI=10.1074/jbc.272.39.24522;
RA   Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., Park M.S.;
RT   "The DNA repair endonuclease XPG binds to proliferating cell nuclear
RT   antigen (PCNA) and shares sequence elements with the PCNA-binding
RT   regions of FEN-1 and cyclin-dependent kinase inhibitor p21.";
RL   J. Biol. Chem. 272:24522-24529(1997).
RN   [15]
RP   REVIEW.
RX   PubMed=14726017; DOI=10.1016/j.biochi.2003.10.014;
RA   Clarkson S.G.;
RT   "The XPG story.";
RL   Biochimie 85:1113-1121(2003).
RN   [16]
RP   REVIEW ON VARIANTS XP-G.
RX   PubMed=10447254;
RX   DOI=10.1002/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6;
RA   Cleaver J.E., Thompson L.H., Richardson A.S., States J.C.;
RT   "A summary of mutations in the UV-sensitive disorders: xeroderma
RT   pigmentosum, Cockayne syndrome, and trichothiodystrophy.";
RL   Hum. Mutat. 14:9-22(1999).
RN   [17]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [19]
RP   VARIANT XP-G VAL-792.
RX   PubMed=7951246; DOI=10.1093/hmg/3.6.963;
RA   Nouspikel T., Clarkson S.G.;
RT   "Mutations that disable the DNA repair gene XPG in a Xeroderma
RT   pigmentosum group G patient.";
RL   Hum. Mol. Genet. 3:963-967(1994).
RN   [20]
RP   VARIANT XP-G VAL-792.
RX   PubMed=9096355; DOI=10.1073/pnas.94.7.3116;
RA   Nouspikel T., Lalle P., Leadon S.A., Cooper P.K., Clarkson S.G.;
RT   "A common mutational pattern in Cockayne syndrome patients from
RT   Xeroderma pigmentosum group G: implications for a second XPG
RT   function.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3116-3121(1997).
RN   [21]
RP   VARIANT XP-G HIS-72.
RX   PubMed=11228268; DOI=10.1203/00006450-200103000-00016;
RA   Zafeiriou D.I., Thorel F., Andreou A., Kleijer W.J., Raams A.,
RA   Garritsen V.H., Gombakis N., Jaspers N.G.J., Clarkson S.G.;
RT   "Xeroderma pigmentosum group G with severe neurological involvement
RT   and features of Cockayne syndrome in infancy.";
RL   Pediatr. Res. 49:407-412(2001).
RN   [22]
RP   VARIANT XP-G PRO-858.
RX   PubMed=11841555; DOI=10.1046/j.0022-202x.2001.01673.x;
RA   Lalle P., Nouspikel T., Constantinou A., Thorel F., Clarkson S.G.;
RT   "The founding members of xeroderma pigmentosum group G produce XPG
RT   protein with severely impaired endonuclease activity.";
RL   J. Invest. Dermatol. 118:344-351(2002).
RN   [23]
RP   VARIANT XP-G THR-874.
RX   PubMed=12060391; DOI=10.1046/j.1523-1747.2002.01782.x;
RA   Emmert S., Slor H., Busch D.B., Batko S., Albert R.B., Coleman D.,
RA   Khan S.G., Abu-Libdeh B., DiGiovanna J.J., Cunningham B.B., Lee M.M.,
RA   Crollick J., Inui H., Ueda T., Hedayati M., Grossman L., Shahlavi T.,
RA   Cleaver J.E., Kraemer K.H.;
RT   "Relationship of neurologic degeneration to genotype in three
RT   xeroderma pigmentosum group G patients.";
RL   J. Invest. Dermatol. 118:972-982(2002).
CC   -!- FUNCTION: Single-stranded structure-specific DNA endonuclease
CC       involved in DNA excision repair. Makes the 3'incision in DNA
CC       nucleotide excision repair (NER). Acts as a cofactor for a DNA
CC       glycosylase that removes oxidized pyrimidines from DNA. May also
CC       be involved in transcription-coupled repair of this kind of
CC       damage, in transcription by RNA polymerase II, and perhaps in
CC       other processes too.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. They probably participate
CC       in the reaction catalyzed by the enzyme. May bind an additional
CC       third magnesium ion after substrate binding. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with PCNA. {ECO:0000269|PubMed:9305916}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7651464}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P28715-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P28715-2; Sequence=VSP_035380;
CC       Name=3;
CC         IsoId=P28715-3; Sequence=VSP_053828, VSP_053829;
CC         Note=No experimental confirmation available. Includes a cryptic
CC         exon found in intron 6.;
CC   -!- DISEASE: Xeroderma pigmentosum complementation group G (XP-G)
CC       [MIM:278780]: An autosomal recessive pigmentary skin disorder
CC       characterized by solar hypersensitivity of the skin, high
CC       predisposition for developing cancers on areas exposed to sunlight
CC       and, in some cases, neurological abnormalities. The skin develops
CC       marked freckling and other pigmentation abnormalities. Some XP-G
CC       patients present features of Cockayne syndrome, cachectic
CC       dwarfism, pigmentary retinopathy, ataxia, decreased nerve
CC       conduction velocities. The phenotype combining xeroderma
CC       pigmentosum and Cockayne syndrome traits is referred to as XP-CS
CC       complex. {ECO:0000269|PubMed:11228268,
CC       ECO:0000269|PubMed:11841555, ECO:0000269|PubMed:12060391,
CC       ECO:0000269|PubMed:7951246, ECO:0000269|PubMed:9096355}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG
CC       subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Allelic variations of the XP genes;
CC       URL="http://www.xpmutations.org/";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/XPGID300.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ercc5/";
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DR   EMBL; X69978; CAA49598.1; -; mRNA.
DR   EMBL; D16305; BAA03812.1; -; mRNA.
DR   EMBL; L20046; AAC37533.1; -; mRNA.
DR   EMBL; AF255436; AAF89178.1; -; Genomic_DNA.
DR   EMBL; AF255431; AAF89178.1; JOINED; Genomic_DNA.
DR   EMBL; AF255433; AAF89178.1; JOINED; Genomic_DNA.
DR   EMBL; AF255434; AAF89178.1; JOINED; Genomic_DNA.
DR   EMBL; AF255435; AAF89178.1; JOINED; Genomic_DNA.
DR   EMBL; AF255442; AAF89179.1; -; Genomic_DNA.
DR   EMBL; AF255431; AAF89179.1; JOINED; Genomic_DNA.
DR   EMBL; AF255433; AAF89179.1; JOINED; Genomic_DNA.
DR   EMBL; AF255434; AAF89179.1; JOINED; Genomic_DNA.
DR   EMBL; AF255435; AAF89179.1; JOINED; Genomic_DNA.
DR   EMBL; AF255436; AAF89179.1; JOINED; Genomic_DNA.
DR   EMBL; AF255437; AAF89179.1; JOINED; Genomic_DNA.
DR   EMBL; AF255438; AAF89179.1; JOINED; Genomic_DNA.
DR   EMBL; AF255439; AAF89179.1; JOINED; Genomic_DNA.
DR   EMBL; AF255440; AAF89179.1; JOINED; Genomic_DNA.
DR   EMBL; AF255441; AAF89179.1; JOINED; Genomic_DNA.
DR   EMBL; AF462447; AAP97715.1; -; mRNA.
DR   EMBL; AF550128; AAN46091.1; -; Genomic_DNA.
DR   EMBL; AL157769; CAI14530.1; -; Genomic_DNA.
DR   EMBL; AL157769; CAI14531.1; -; Genomic_DNA.
DR   EMBL; BC031522; AAH31522.1; -; mRNA.
DR   EMBL; X71341; CAA50481.1; -; Genomic_DNA.
DR   EMBL; X71342; CAA50481.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS32004.1; -. [P28715-1]
DR   PIR; I58009; I58009.
DR   PIR; S35993; S35993.
DR   RefSeq; NP_000114.2; NM_000123.3.
DR   UniGene; Hs.258429; -.
DR   ProteinModelPortal; P28715; -.
DR   SMR; P28715; 2-113, 711-981.
DR   BioGrid; 108385; 14.
DR   DIP; DIP-750N; -.
DR   IntAct; P28715; 4.
DR   MINT; MINT-192239; -.
DR   STRING; 9606.ENSP00000347978; -.
DR   BindingDB; P28715; -.
DR   ChEMBL; CHEMBL4736; -.
DR   PhosphoSite; P28715; -.
DR   BioMuta; ERCC5; -.
DR   DMDM; 205371791; -.
DR   MaxQB; P28715; -.
DR   PaxDb; P28715; -.
DR   PRIDE; P28715; -.
DR   DNASU; 2073; -.
DR   Ensembl; ENST00000355739; ENSP00000347978; ENSG00000134899. [P28715-1]
DR   Ensembl; ENST00000375954; ENSP00000365121; ENSG00000134899. [P28715-2]
DR   Ensembl; ENST00000535557; ENSP00000442117; ENSG00000134899. [P28715-3]
DR   GeneID; 2073; -.
DR   KEGG; hsa:2073; -.
DR   UCSC; uc001vpw.3; human. [P28715-1]
DR   CTD; 2073; -.
DR   GeneCards; ERCC5; -.
DR   GeneReviews; ERCC5; -.
DR   HGNC; HGNC:3437; ERCC5.
DR   HPA; HPA045845; -.
DR   HPA; HPA050374; -.
DR   MIM; 133530; gene.
DR   MIM; 278780; phenotype.
DR   neXtProt; NX_P28715; -.
DR   Orphanet; 1466; COFS syndrome.
DR   Orphanet; 276267; Xeroderma pigmentosum complementation group G.
DR   PharmGKB; PA27851; -.
DR   eggNOG; KOG2520; Eukaryota.
DR   eggNOG; COG0258; LUCA.
DR   GeneTree; ENSGT00640000091542; -.
DR   HOVERGEN; HBG051501; -.
DR   InParanoid; P28715; -.
DR   KO; K10846; -.
DR   OMA; EAQCCEL; -.
DR   OrthoDB; EOG72ZCD4; -.
DR   PhylomeDB; P28715; -.
DR   TreeFam; TF101235; -.
DR   Reactome; R-HSA-110302; Formation of transcription-coupled NER (TC-NER) repair complex.
DR   Reactome; R-HSA-110304; Dual incision reaction in TC-NER.
DR   Reactome; R-HSA-73935; Formation of incision complex in GG-NER.
DR   Reactome; R-HSA-73941; Dual incision reaction in GG-NER.
DR   GeneWiki; ERCC5; -.
DR   GenomeRNAi; 2073; -.
DR   NextBio; 8433; -.
DR   PRO; PR:P28715; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   Bgee; P28715; -.
DR   CleanEx; HS_ERCC5; -.
DR   ExpressionAtlas; P28715; baseline and differential.
DR   Genevisible; P28715; HS.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000405; F:bubble DNA binding; IDA:UniProtKB.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR   GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0004519; F:endonuclease activity; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; TAS:Reactome.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0006289; P:nucleotide-excision repair; TAS:Reactome.
DR   GO; GO:0000718; P:nucleotide-excision repair, DNA damage removal; TAS:Reactome.
DR   GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; IDA:UniProtKB.
DR   GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR   GO; GO:0010225; P:response to UV-C; IMP:UniProtKB.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:UniProtKB.
DR   GO; GO:0009650; P:UV protection; IGI:MGI.
DR   Gene3D; 3.40.50.1010; -; 2.
DR   InterPro; IPR020045; 5-3_exonuclease_C.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN_domain-like.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   PRINTS; PR00066; XRODRMPGMNTG.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; SSF47807; 2.
DR   SUPFAM; SSF88723; SSF88723; 2.
DR   TIGRFAMs; TIGR00600; rad2; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cockayne syndrome;
KW   Complete proteome; Deafness; Disease mutation; DNA damage; DNA repair;
KW   DNA-binding; Dwarfism; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Xeroderma pigmentosum.
FT   CHAIN         1   1186       DNA repair protein complementing XP-G
FT                                cells.
FT                                /FTId=PRO_0000154031.
FT   REGION        1     95       N-domain.
FT   REGION      753    881       I-domain.
FT   REGION      981   1009       Interaction with PCNA.
FT   MOTIF      1057   1073       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   METAL        30     30       Magnesium 1. {ECO:0000250}.
FT   METAL        77     77       Magnesium 1. {ECO:0000250}.
FT   METAL       789    789       Magnesium 1. {ECO:0000250}.
FT   METAL       791    791       Magnesium 1. {ECO:0000250}.
FT   METAL       810    810       Magnesium 2. {ECO:0000250}.
FT   METAL       812    812       Magnesium 2. {ECO:0000250}.
FT   METAL       861    861       Magnesium 2. {ECO:0000250}.
FT   MOD_RES       8      8       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     384    384       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P35689}.
FT   MOD_RES     705    705       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P35689}.
FT   VAR_SEQ       1    767       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_035380.
FT   VAR_SEQ     225    232       ESDDFSQY -> VYLPLLQP (in isoform 3).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_053828.
FT   VAR_SEQ     233   1186       Missing (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_053829.
FT   VARIANT      72     72       P -> H (in XP-G; combined with features
FT                                of Cockayne syndrome).
FT                                {ECO:0000269|PubMed:11228268}.
FT                                /FTId=VAR_015280.
FT   VARIANT     145    145       V -> I (in dbSNP:rs4987063).
FT                                /FTId=VAR_020431.
FT   VARIANT     181    181       H -> R (in dbSNP:rs4150295).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_023120.
FT   VARIANT     254    254       M -> V (in dbSNP:rs1047769).
FT                                {ECO:0000269|PubMed:7510366,
FT                                ECO:0000269|PubMed:8413238,
FT                                ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
FT                                /FTId=VAR_007732.
FT   VARIANT     256    256       Q -> R (in dbSNP:rs4150313).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_020432.
FT   VARIANT     311    311       S -> C (in dbSNP:rs2307491).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_014829.
FT   VARIANT     399    399       E -> K (in dbSNP:rs4150315).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_023121.
FT   VARIANT     529    529       C -> S (in dbSNP:rs2227869).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_020433.
FT   VARIANT     590    590       V -> I (in dbSNP:rs4150318).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_023122.
FT   VARIANT     597    597       V -> L (in dbSNP:rs4150319).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_023123.
FT   VARIANT     670    670       F -> L (in dbSNP:rs1803542).
FT                                /FTId=VAR_046373.
FT   VARIANT     680    680       Q -> R (in dbSNP:rs4987168).
FT                                /FTId=VAR_020434.
FT   VARIANT     792    792       A -> V (in XP-G; mild form).
FT                                {ECO:0000269|PubMed:7951246,
FT                                ECO:0000269|PubMed:9096355}.
FT                                /FTId=VAR_007733.
FT   VARIANT     858    858       L -> P (in XP-G; reduced stability and
FT                                greatly impaired endonuclease activity).
FT                                {ECO:0000269|PubMed:11841555}.
FT                                /FTId=VAR_017097.
FT   VARIANT     874    874       A -> T (in XP-G; mild form; residual
FT                                activity; dbSNP:rs28929496).
FT                                {ECO:0000269|PubMed:12060391}.
FT                                /FTId=VAR_017096.
FT   VARIANT     879    879       N -> S (in dbSNP:rs4150342).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_020435.
FT   VARIANT    1009   1009       R -> H (in dbSNP:rs4150387).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_023124.
FT   VARIANT    1053   1053       G -> R (in dbSNP:rs9514066).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:7510366,
FT                                ECO:0000269|PubMed:8413238,
FT                                ECO:0000269|PubMed:8483504,
FT                                ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
FT                                /FTId=VAR_046374.
FT   VARIANT    1080   1080       G -> Q (requires 2 nucleotide
FT                                substitutions). {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_023125.
FT   VARIANT    1080   1080       G -> R (in dbSNP:rs9514067).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:7510366,
FT                                ECO:0000269|PubMed:8413238,
FT                                ECO:0000269|PubMed:8483504,
FT                                ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
FT                                /FTId=VAR_046375.
FT   VARIANT    1104   1104       D -> H (in dbSNP:rs17655).
FT                                {ECO:0000269|PubMed:8483504}.
FT                                /FTId=VAR_007734.
FT   VARIANT    1119   1119       A -> V (in dbSNP:rs2227871).
FT                                /FTId=VAR_020436.
FT   CONFLICT     55     55       L -> P (in Ref. 2; BAA03812).
FT                                {ECO:0000305}.
FT   CONFLICT    120    122       KTA -> QTS (in Ref. 2; BAA03812).
FT                                {ECO:0000305}.
FT   CONFLICT    126    126       K -> Q (in Ref. 2; BAA03812).
FT                                {ECO:0000305}.
FT   CONFLICT    264    266       RQY -> SSH (in Ref. 2; BAA03812).
FT                                {ECO:0000305}.
FT   CONFLICT    760    760       I -> F (in Ref. 2; BAA03812).
FT                                {ECO:0000305}.
FT   CONFLICT    796    796       I -> V (in Ref. 2; BAA03812).
FT                                {ECO:0000305}.
FT   CONFLICT    864    872       EGIPTVGCV -> GNTNCGLC (in Ref. 2;
FT                                BAA03812). {ECO:0000305}.
FT   CONFLICT    959    959       R -> S (in Ref. 2; BAA03812).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1186 AA;  133108 MW;  B0A844D617C53F2E CRC64;
     MGVQGLWKLL ECSGRQVSPE ALEGKILAVD ISIWLNQALK GVRDRHGNSI ENPHLLTLFH
     RLCKLLFFRI RPIFVFDGDA PLLKKQTLVK RRQRKDLASS DSRKTTEKLL KTFLKRQAIK
     TAFRSKRDEA LPSLTQVRRE NDLYVLPPLQ EEEKHSSEEE DEKEWQERMN QKQALQEEFF
     HNPQAIDIES EDFSSLPPEV KHEILTDMKE FTKRRRTLFE AMPEESDDFS QYQLKGLLKK
     NYLNQHIEHV QKEMNQQHSG HIRRQYEDEG GFLKEVESRR VVSEDTSHYI LIKGIQAKTV
     AEVDSESLPS SSKMHGMSFD VKSSPCEKLK TEKEPDATPP SPRTLLAMQA ALLGSSSEEE
     LESENRRQAR GRNAPAAVDE GSISPRTLSA IKRALDDDED VKVCAGDDVQ TGGPGAEEMR
     INSSTENSDE GLKVRDGKGI PFTATLASSS VNSAEEHVAS TNEGREPTDS VPKEQMSLVH
     VGTEAFPISD ESMIKDRKDR LPLESAVVRH SDAPGLPNGR ELTPASPTCT NSVSKNETHA
     EVLEQQNELC PYESKFDSSL LSSDDETKCK PNSASEVIGP VSLQETSSIV SVPSEAVDNV
     ENVVSFNAKE HENFLETIQE QQTTESAGQD LISIPKAVEP MEIDSEESES DGSFIEVQSV
     ISDEELQAEF PETSKPPSEQ GEEELVGTRE GEAPAESESL LRDNSERDDV DGEPQEAEKD
     AEDSLHEWQD INLEELETLE SNLLAQQNSL KAQKQQQERI AATVTGQMFL ESQELLRLFG
     IPYIQAPMEA EAQCAILDLT DQTSGTITDD SDIWLFGARH VYRNFFNKNK FVEYYQYVDF
     HNQLGLDRNK LINLAYLLGS DYTEGIPTVG CVTAMEILNE FPGHGLEPLL KFSEWWHEAQ
     KNPKIRPNPH DTKVKKKLRT LQLTPGFPNP AVAEAYLKPV VDDSKGSFLW GKPDLDKIRE
     FCQRYFGWNR TKTDESLFPV LKQLDAQQTQ LRIDSFFRLA QQEKEDAKRI KSQRLNRAVT
     CMLRKEKEAA ASEIEAVSVA MEKEFELLDK AKGKTQKRGI TNTLEESSSL KRKRLSDSKG
     KNTCGGFLGE TCLSESSDGS SSEDAESSSL MNVQRRTAAK EPKTSASDSQ NSVKEAPVKN
     GGATTSSSSD SDDDGGKEKM VLVTARSVFG KKRRKLRRAR GRKRKT
//
ID   FEN1_HUMAN              Reviewed;         380 AA.
AC   P39748;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   11-NOV-2015, entry version 159.
DE   RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
DE            Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140};
DE   AltName: Full=DNase IV;
DE   AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
DE   AltName: Full=Maturation factor 1;
DE            Short=MF1;
DE            Short=hFEN-1;
GN   Name=FEN1 {ECO:0000255|HAMAP-Rule:MF_03140}; Synonyms=RAD2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8007985;
RA   Murray J.M., Tavassoli M., Al-Harithy R., Sheldrick K.S.,
RA   Lehmann A.R., Carr A.M., Watts F.Z.;
RT   "Structural and functional conservation of the human homolog of the
RT   Schizosaccharomyces pombe rad2 gene, which is required for chromosome
RT   segregation and recovery from DNA damage.";
RL   Mol. Cell. Biol. 14:4878-4888(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=7774922; DOI=10.1016/0888-7543(95)80129-A;
RA   Hiraoka L.R., Harrington J.J., Gerhard D.S., Lieber M.R., Hsieh C.-L.;
RT   "Sequence of human FEN-1, a structure-specific endonuclease, and
RT   chromosomal localization of the gene (FEN1) in mouse and human.";
RL   Genomics 25:220-225(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=7961795;
RA   Robins P., Pappin D.J.C., Wood R.D., Lindahl T.;
RT   "Structural and functional homology between mammalian DNase IV and the
RT   5'-nuclease domain of Escherichia coli DNA polymerase I.";
RL   J. Biol. Chem. 269:28535-28538(1994).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE-BINDING SITES, AND MUTAGENESIS
RP   OF ASP-34; ASP-86; ARG-103; GLU-158; ASP-179; ASP-181; GLY-231 AND
RP   ASP-233.
RX   PubMed=8621570; DOI=10.1074/jbc.271.16.9173;
RA   Shen B., Nolan J.P., Sklar L.A., Park M.S.;
RT   "Essential amino acids for substrate binding and catalysis of human
RT   flap endonuclease 1.";
RL   J. Biol. Chem. 271:9173-9176(1996).
RN   [8]
RP   INTERACTION WITH PCNA.
RX   PubMed=9305916; DOI=10.1074/jbc.272.39.24522;
RA   Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., Park M.S.;
RT   "The DNA repair endonuclease XPG binds to proliferating cell nuclear
RT   antigen (PCNA) and shares sequence elements with the PCNA-binding
RT   regions of FEN-1 and cyclin-dependent kinase inhibitor p21.";
RL   J. Biol. Chem. 272:24522-24529(1997).
RN   [9]
RP   FUNCTION.
RX   PubMed=10744741; DOI=10.1074/jbc.275.14.10498;
RA   Tom S., Henricksen L.A., Bambara R.A.;
RT   "Mechanism whereby proliferating cell nuclear antigen stimulates flap
RT   endonuclease 1.";
RL   J. Biol. Chem. 275:10498-10505(2000).
RN   [10]
RP   INTERACTION WITH P300, AND ACETYLATION AT LYS-354; LYS-375; LYS-377
RP   AND LYS-380.
RX   PubMed=11430825; DOI=10.1016/S1097-2765(01)00272-6;
RA   Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P.,
RA   Hubscher U., Hottiger M.O.;
RT   "Regulation of human flap endonuclease-1 activity by acetylation
RT   through the transcriptional coactivator p300.";
RL   Mol. Cell 7:1221-1231(2001).
RN   [11]
RP   FUNCTION, SUBSTRATE-BINDING SITES ARG-47 AND ARG-70, AND MUTAGENESIS
RP   OF ARG-29; ARG-47; ARG-70; ARG-73 AND LYS-80.
RX   PubMed=11986308; DOI=10.1074/jbc.M111941200;
RA   Qiu J., Bimston D.N., Partikian A., Shen B.;
RT   "Arginine residues 47 and 70 of human flap endonuclease-1 are involved
RT   in DNA substrate interactions and cleavage site determination.";
RL   J. Biol. Chem. 277:24659-24666(2002).
RN   [12]
RP   INTERACTION WITH DDX11.
RX   PubMed=18499658; DOI=10.1074/jbc.M802696200;
RA   Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S.,
RA   Hurwitz J.;
RT   "Studies with the human cohesin establishment factor, ChlR1.
RT   Association of ChlR1 with Ctf18-RFC and Fen1.";
RL   J. Biol. Chem. 283:20925-20936(2008).
RN   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF
RP   SER-187.
RX   PubMed=18443037; DOI=10.1128/MCB.00200-08;
RA   Guo Z., Qian L., Liu R., Dai H., Zhou M., Zheng L., Shen B.;
RT   "Nucleolar localization and dynamic roles of flap endonuclease 1 in
RT   ribosomal DNA replication and damage repair.";
RL   Mol. Cell. Biol. 28:4310-4319(2008).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80 AND LYS-375, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [15]
RP   FUNCTION, MUTAGENESIS OF ARG-192, METHYLATION AT ARG-19; ARG-100;
RP   ARG-104 AND ARG-192, AND PHOSPHORYLATION AT SER-187.
RX   PubMed=20729856; DOI=10.1038/nchembio.422;
RA   Guo Z., Zheng L., Xu H., Dai H., Zhou M., Pascua M.R., Chen Q.M.,
RA   Shen B.;
RT   "Methylation of FEN1 suppresses nearby phosphorylation and facilitates
RT   PCNA binding.";
RL   Nat. Chem. Biol. 6:766-773(2010).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND THR-364, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [19]
RP   ALTERNATIVE INITIATION (ISOFORM FENMIT), AND SUBCELLULAR LOCATION
RP   (ISOFORM FENMIT).
RX   PubMed=23675412; DOI=10.1371/journal.pone.0062340;
RA   Kazak L., Reyes A., He J., Wood S.R., Brea-Calvo G., Holen T.T.,
RA   Holt I.J.;
RT   "A cryptic targeting signal creates a mitochondrial FEN1 isoform with
RT   tailed R-loop binding properties.";
RL   PLoS ONE 8:E62340-E62340(2013).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 331-350.
RX   PubMed=15576034; DOI=10.1016/j.str.2004.09.018;
RA   Bruning J.B., Shamoo Y.;
RT   "Structural and thermodynamic analysis of human PCNA with peptides
RT   derived from DNA polymerase-delta p66 subunit and flap endonuclease-
RT   1.";
RL   Structure 12:2209-2219(2004).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 2-380 IN COMPLEX WITH PCNA.
RX   PubMed=15616578; DOI=10.1038/sj.emboj.7600519;
RA   Sakurai S., Kitano K., Yamaguchi H., Hamada K., Okada K., Fukuda K.,
RA   Uchida M., Ohtsuka E., Morioka H., Hakoshima T.;
RT   "Structural basis for recruitment of human flap endonuclease 1 to
RT   PCNA.";
RL   EMBO J. 24:683-693(2005).
CC   -!- FUNCTION: Structure-specific nuclease with 5'-flap endonuclease
CC       and 5'-3' exonuclease activities involved in DNA replication and
CC       repair. During DNA replication, cleaves the 5'-overhanging flap
CC       structure that is generated by displacement synthesis when DNA
CC       polymerase encounters the 5'-end of a downstream Okazaki fragment.
CC       It enters the flap from the 5'-end and then tracks to cleave the
CC       flap base, leaving a nick for ligation. Also involved in the long
CC       patch base excision repair (LP-BER) pathway, by cleaving within
CC       the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a
CC       genome stabilization factor that prevents flaps from equilibrating
CC       into structurs that lead to duplications and deletions. Also
CC       possesses 5'-3' exonuclease activity on nicked or gapped double-
CC       stranded DNA, and exhibits RNase H activity. Also involved in
CC       replication and repair of rDNA and in repairing mitochondrial DNA.
CC       {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:10744741,
CC       ECO:0000269|PubMed:11986308, ECO:0000269|PubMed:18443037,
CC       ECO:0000269|PubMed:20729856, ECO:0000269|PubMed:7961795,
CC       ECO:0000269|PubMed:8621570}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 2 magnesium ions per subunit. They probably participate
CC       in the reaction catalyzed by the enzyme. May bind an additional
CC       third magnesium ion after substrate binding.;
CC   -!- SUBUNIT: Interacts with PCNA. Three molecules of FEN1 bind to one
CC       PCNA trimer with each molecule binding to one PCNA monomer. PCNA
CC       stimulates the nuclease activity without altering cleavage
CC       specificity. The C-terminal domain binds EP300. Can bind
CC       simultaneously to both PCNA and EP300. Interacts with DDX11.
CC       {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:11430825,
CC       ECO:0000269|PubMed:15616578, ECO:0000269|PubMed:18499658,
CC       ECO:0000269|PubMed:9305916}.
CC   -!- INTERACTION:
CC       P54132:BLM; NbExp=4; IntAct=EBI-707816, EBI-621372;
CC       Q96NY9:MUS81; NbExp=5; IntAct=EBI-707816, EBI-2370806;
CC       P12004:PCNA; NbExp=4; IntAct=EBI-707816, EBI-358311;
CC       Q14191:WRN; NbExp=9; IntAct=EBI-707816, EBI-368417;
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus. Nucleus,
CC       nucleoplasm. Note=Resides mostly in the nucleoli and relocalizes
CC       to the nucleoplasm upon DNA damage.
CC   -!- SUBCELLULAR LOCATION: Isoform FENMIT: Mitochondrion
CC       {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:23675412}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1;
CC         IsoId=P39748-1; Sequence=Displayed;
CC       Name=FENMIT;
CC         IsoId=P39748-2; Sequence=VSP_047520;
CC         Note=No nuclease activity. Binds preferentially to RNA flap
CC         structures and R-loops.;
CC   -!- PTM: Acetylated by EP300. Acetylation inhibits both endonuclease
CC       and exonuclease activity. Acetylation also reduces DNA-binding
CC       activity but does not affect interaction with PCNA or EP300.
CC       {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:11430825}.
CC   -!- PTM: Phosphorylation upon DNA damage induces relocalization to the
CC       nuclear plasma. Phosphorylation at Ser-187 by CDK2 occurs during
CC       late S-phase and results in dissociation from PCNA.
CC       {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856}.
CC   -!- PTM: Methylation at Arg-192 by PRMT5 impedes Ser-187
CC       phosphorylation and increases interaction with PCNA.
CC       {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03140}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/fen1/";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/FEN1ID40543ch11q12.html";
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DR   EMBL; X76771; CAA54166.1; -; mRNA.
DR   EMBL; L37374; AAA91331.1; -; mRNA.
DR   EMBL; AF523117; AAM74238.1; -; Genomic_DNA.
DR   EMBL; AC004770; AAC23394.1; -; Genomic_DNA.
DR   EMBL; BC000323; AAH00323.1; -; mRNA.
DR   CCDS; CCDS8010.1; -. [P39748-1]
DR   PIR; A56531; A56531.
DR   RefSeq; NP_004102.1; NM_004111.5. [P39748-1]
DR   UniGene; Hs.409065; -.
DR   PDB; 1U7B; X-ray; 1.88 A; B=331-350.
DR   PDB; 1UL1; X-ray; 2.90 A; X/Y/Z=2-380.
DR   PDB; 3Q8K; X-ray; 2.20 A; A=2-336.
DR   PDB; 3Q8L; X-ray; 2.32 A; A=2-336.
DR   PDB; 3Q8M; X-ray; 2.60 A; A/B=2-336.
DR   PDB; 3UVU; X-ray; 2.38 A; B=352-370.
DR   PDBsum; 1U7B; -.
DR   PDBsum; 1UL1; -.
DR   PDBsum; 3Q8K; -.
DR   PDBsum; 3Q8L; -.
DR   PDBsum; 3Q8M; -.
DR   PDBsum; 3UVU; -.
DR   ProteinModelPortal; P39748; -.
DR   SMR; P39748; 2-336.
DR   BioGrid; 108528; 46.
DR   DIP; DIP-24216N; -.
DR   IntAct; P39748; 15.
DR   MINT; MINT-5004212; -.
DR   STRING; 9606.ENSP00000305480; -.
DR   BindingDB; P39748; -.
DR   ChEMBL; CHEMBL5027; -.
DR   PhosphoSite; P39748; -.
DR   BioMuta; FEN1; -.
DR   DMDM; 729475; -.
DR   MaxQB; P39748; -.
DR   PaxDb; P39748; -.
DR   PeptideAtlas; P39748; -.
DR   PRIDE; P39748; -.
DR   DNASU; 2237; -.
DR   Ensembl; ENST00000305885; ENSP00000305480; ENSG00000168496. [P39748-1]
DR   GeneID; 2237; -.
DR   KEGG; hsa:2237; -.
DR   UCSC; uc001nsg.3; human. [P39748-1]
DR   CTD; 2237; -.
DR   GeneCards; FEN1; -.
DR   HGNC; HGNC:3650; FEN1.
DR   HPA; CAB002262; -.
DR   HPA; HPA006581; -.
DR   HPA; HPA006748; -.
DR   MIM; 600393; gene.
DR   neXtProt; NX_P39748; -.
DR   PharmGKB; PA28090; -.
DR   eggNOG; KOG2519; Eukaryota.
DR   eggNOG; COG0258; LUCA.
DR   HOGENOM; HOG000193853; -.
DR   HOVERGEN; HBG000844; -.
DR   InParanoid; P39748; -.
DR   KO; K04799; -.
DR   OMA; GSQDYDS; -.
DR   OrthoDB; EOG72JWHG; -.
DR   PhylomeDB; P39748; -.
DR   TreeFam; TF105701; -.
DR   Reactome; R-HSA-110362; POLB-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand.
DR   Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-HSA-69166; Removal of the Flap Intermediate.
DR   SignaLink; P39748; -.
DR   ChiTaRS; FEN1; human.
DR   EvolutionaryTrace; P39748; -.
DR   GeneWiki; Flap_structure-specific_endonuclease_1; -.
DR   GenomeRNAi; 2237; -.
DR   NextBio; 9055; -.
DR   PRO; PR:P39748; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; P39748; -.
DR   CleanEx; HS_FEN1; -.
DR   ExpressionAtlas; P39748; baseline and differential.
DR   Genevisible; P39748; HS.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0043234; C:protein complex; IDA:MGI.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IDA:UniProtKB.
DR   GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
DR   GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
DR   GO; GO:0003690; F:double-stranded DNA binding; TAS:ProtInc.
DR   GO; GO:0008309; F:double-stranded DNA exodeoxyribonuclease activity; TAS:ProtInc.
DR   GO; GO:0004519; F:endonuclease activity; TAS:ProtInc.
DR   GO; GO:0004527; F:exonuclease activity; TAS:ProtInc.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR   GO; GO:0030145; F:manganese ion binding; IEA:Ensembl.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0006284; P:base-excision repair; TAS:Reactome.
DR   GO; GO:0006281; P:DNA repair; TAS:Reactome.
DR   GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IDA:UniProtKB.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
DR   GO; GO:0006302; P:double-strand break repair; TAS:ProtInc.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:GOC.
DR   GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:GOC.
DR   GO; GO:0000723; P:telomere maintenance; TAS:Reactome.
DR   GO; GO:0000722; P:telomere maintenance via recombination; TAS:Reactome.
DR   GO; GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
DR   GO; GO:0009650; P:UV protection; TAS:ProtInc.
DR   Gene3D; 3.40.50.1010; -; 1.
DR   HAMAP; MF_00614; Fen; 1.
DR   InterPro; IPR020045; 5-3_exonuclease_C.
DR   InterPro; IPR023426; Flap_endonuc.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN_domain-like.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   PANTHER; PTHR11081; PTHR11081; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; SSF47807; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative initiation; Complete proteome;
KW   Direct protein sequencing; DNA damage; DNA repair; DNA replication;
KW   Endonuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Methylation; Mitochondrion; Nuclease; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1    380       Flap endonuclease 1.
FT                                /FTId=PRO_0000154069.
FT   REGION        1    104       N-domain.
FT   REGION      122    253       I-domain.
FT   REGION      336    344       Interaction with PCNA.
FT   METAL        34     34       Magnesium 1.
FT   METAL        86     86       Magnesium 1.
FT   METAL       158    158       Magnesium 1.
FT   METAL       160    160       Magnesium 1.
FT   METAL       179    179       Magnesium 2.
FT   METAL       181    181       Magnesium 2.
FT   METAL       233    233       Magnesium 2.
FT   BINDING      47     47       DNA substrate.
FT   BINDING      70     70       DNA substrate.
FT   BINDING     158    158       DNA substrate.
FT   BINDING     231    231       DNA substrate.
FT   BINDING     233    233       DNA substrate.
FT   MOD_RES      19     19       Symmetric dimethylarginine; by PRMT5.
FT                                {ECO:0000255|HAMAP-Rule:MF_03140,
FT                                ECO:0000269|PubMed:20729856}.
FT   MOD_RES      80     80       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     100    100       Symmetric dimethylarginine; by PRMT5.
FT                                {ECO:0000255|HAMAP-Rule:MF_03140,
FT                                ECO:0000269|PubMed:20729856}.
FT   MOD_RES     104    104       Symmetric dimethylarginine; by PRMT5.
FT                                {ECO:0000255|HAMAP-Rule:MF_03140,
FT                                ECO:0000269|PubMed:20729856}.
FT   MOD_RES     187    187       Phosphoserine; by CDK2.
FT                                {ECO:0000255|HAMAP-Rule:MF_03140,
FT                                ECO:0000269|PubMed:20729856}.
FT   MOD_RES     192    192       Symmetric dimethylarginine; by PRMT5.
FT                                {ECO:0000255|HAMAP-Rule:MF_03140,
FT                                ECO:0000269|PubMed:20729856}.
FT   MOD_RES     197    197       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     354    354       N6-acetyllysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140,
FT                                ECO:0000269|PubMed:11430825}.
FT   MOD_RES     364    364       Phosphothreonine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     375    375       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861,
FT                                ECO:0000255|HAMAP-Rule:MF_03140,
FT                                ECO:0000269|PubMed:11430825}.
FT   MOD_RES     377    377       N6-acetyllysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140,
FT                                ECO:0000269|PubMed:11430825}.
FT   MOD_RES     380    380       N6-acetyllysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140,
FT                                ECO:0000269|PubMed:11430825}.
FT   VAR_SEQ       1     64       Missing (in isoform FENMIT).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_047520.
FT   MUTAGEN      29     29       R->A: No significant effect on
FT                                exonuclease activity or flap endonuclease
FT                                activity. {ECO:0000269|PubMed:11986308}.
FT   MUTAGEN      34     34       D->A: Loss of flap endonuclease activity
FT                                but substrate binding activity is
FT                                retained. {ECO:0000269|PubMed:8621570}.
FT   MUTAGEN      47     47       R->A: Significantly reduced exonuclease
FT                                activity and reduced substrate binding.
FT                                The positions of the cleavage sites are
FT                                also shifted.
FT                                {ECO:0000269|PubMed:11986308}.
FT   MUTAGEN      70     70       R->A: Loss of exonuclease activity and
FT                                reduced endonuclease activity. Reduced
FT                                substrate binding.
FT                                {ECO:0000269|PubMed:11986308}.
FT   MUTAGEN      73     73       R->A: No significant effect on
FT                                exonuclease activity or flap endonuclease
FT                                activity. {ECO:0000269|PubMed:11986308}.
FT   MUTAGEN      80     80       K->A: No significant effect on
FT                                exonuclease activity or flap endonuclease
FT                                activity. {ECO:0000269|PubMed:11986308}.
FT   MUTAGEN      86     86       D->A: Loss of flap endonuclease activity
FT                                but substrate binding activity is
FT                                retained. {ECO:0000269|PubMed:8621570}.
FT   MUTAGEN     103    103       R->A: No effect on flap endonuclease
FT                                activity or substrate binding.
FT                                {ECO:0000269|PubMed:8621570}.
FT   MUTAGEN     158    158       E->A: Loss of flap endonuclease activity
FT                                and substrate binding.
FT                                {ECO:0000269|PubMed:8621570}.
FT   MUTAGEN     179    179       D->A: No effect on flap endonuclease
FT                                activity or substrate binding.
FT                                {ECO:0000269|PubMed:8621570}.
FT   MUTAGEN     181    181       D->A: Loss of flap endonuclease activity
FT                                but substrate binding activity is
FT                                retained. {ECO:0000269|PubMed:8621570}.
FT   MUTAGEN     187    187       S->A: Fails to translocate from nucleoli
FT                                to the nuclear plasma.
FT                                {ECO:0000269|PubMed:18443037}.
FT   MUTAGEN     187    187       S->D: Diminishes nucleolar localization.
FT                                {ECO:0000269|PubMed:18443037}.
FT   MUTAGEN     192    192       R->K: Impairs ability to localize to
FT                                sites of DNA replication or repair.
FT                                {ECO:0000269|PubMed:20729856}.
FT   MUTAGEN     231    231       G->A: Loss of flap endonuclease activity
FT                                and substrate binding.
FT                                {ECO:0000269|PubMed:8621570}.
FT   MUTAGEN     233    233       D->A: Loss of flap endonuclease activity
FT                                and substrate binding.
FT                                {ECO:0000269|PubMed:8621570}.
FT   HELIX         6     13       {ECO:0000244|PDB:3Q8K}.
FT   HELIX        15     17       {ECO:0000244|PDB:3Q8K}.
FT   STRAND       18     22       {ECO:0000244|PDB:3Q8K}.
FT   HELIX        23     26       {ECO:0000244|PDB:3Q8K}.
FT   STRAND       30     34       {ECO:0000244|PDB:3Q8K}.
FT   HELIX        35     45       {ECO:0000244|PDB:3Q8K}.
FT   STRAND       47     52       {ECO:0000244|PDB:3Q8M}.
FT   HELIX        62     75       {ECO:0000244|PDB:3Q8K}.
FT   TURN         76     78       {ECO:0000244|PDB:3Q8K}.
FT   STRAND       80     85       {ECO:0000244|PDB:3Q8K}.
FT   HELIX        91     93       {ECO:0000244|PDB:3Q8K}.
FT   HELIX        94    115       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       120    129       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       135    148       {ECO:0000244|PDB:3Q8K}.
FT   STRAND      152    154       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       159    168       {ECO:0000244|PDB:3Q8K}.
FT   STRAND      171    176       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       181    184       {ECO:0000244|PDB:3Q8K}.
FT   STRAND      188    193       {ECO:0000244|PDB:3Q8K}.
FT   STRAND      203    208       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       209    216       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       220    230       {ECO:0000244|PDB:3Q8K}.
FT   STRAND      233    235       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       243    253       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       256    262       {ECO:0000244|PDB:3Q8K}.
FT   TURN        265    267       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       276    284       {ECO:0000244|PDB:3Q8K}.
FT   TURN        291    293       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       303    310       {ECO:0000244|PDB:3Q8K}.
FT   TURN        311    314       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       318    335       {ECO:0000244|PDB:3Q8K}.
FT   HELIX       340    342       {ECO:0000244|PDB:1U7B}.
FT   STRAND      344    351       {ECO:0000244|PDB:1UL1}.
SQ   SEQUENCE   380 AA;  42593 MW;  5154F2F6E57592C5 CRC64;
     MGIQGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG DVLQNEEGET
     TSHLMGMFYR TIRMMENGIK PVYVFDGKPP QLKSGELAKR SERRAEAEKQ LQQAQAAGAE
     QEVEKFTKRL VKVTKQHNDE CKHLLSLMGI PYLDAPSEAE ASCAALVKAG KVYAAATEDM
     DCLTFGSPVL MRHLTASEAK KLPIQEFHLS RILQELGLNQ EQFVDLCILL GSDYCESIRG
     IGPKRAVDLI QKHKSIEEIV RRLDPNKYPV PENWLHKEAH QLFLEPEVLD PESVELKWSE
     PNEEELIKFM CGEKQFSEER IRSGVKRLSK SRQGSTQGRL DDFFKVTGSL SSAKRKEPEP
     KGSTKKKAKT GAAGKFKRGK
//
ID   FEN1_YEAST              Reviewed;         382 AA.
AC   P26793; D6VXH5;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   11-NOV-2015, entry version 145.
DE   RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
DE            Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140};
DE   AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
DE   AltName: Full=RAD2 homolog nuclease 1;
DE            Short=RTH1 nuclease;
DE   AltName: Full=Structure-specific endonuclease RAD27;
GN   Name=RAD27 {ECO:0000255|HAMAP-Rule:MF_03140};
GN   Synonyms=FEN1 {ECO:0000255|HAMAP-Rule:MF_03140}, RTH1;
GN   OrderedLocusNames=YKL113C; ORFNames=YKL510;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1561835; DOI=10.1002/yea.320080207;
RA   Jacquier A., Legrain P., Dujon B.;
RT   "Sequence of a 10.7 kb segment of yeast chromosome XI identifies the
RT   APN1 and the BAF1 loci and reveals one tRNA gene and several new open
RT   reading frames including homologs to RAD2 and kinases.";
RL   Yeast 8:121-132(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
RA   Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
RA   Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
RA   Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   PROTEIN SEQUENCE OF 284-298, FUNCTION, AND EXONUCLEASE AND RNASE H
RP   ACTIVITIES.
RX   PubMed=9166764; DOI=10.1021/bi962889v;
RA   Zhu F.X., Biswas E.E., Biswas S.B.;
RT   "Purification and characterization of the DNA polymerase alpha
RT   associated exonuclease: the RTH1 gene product.";
RL   Biochemistry 36:5947-5954(1997).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=7926735; DOI=10.1101/gad.8.11.1344;
RA   Harrington J.J., Lieber M.R.;
RT   "Functional domains within FEN-1 and RAD2 define a family of
RT   structure-specific endonucleases: implications for nucleotide excision
RT   repair.";
RL   Genes Dev. 8:1344-1355(1994).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=7814325;
RA   Reagan M.S., Pittenger C., Siede W., Friedberg E.C.;
RT   "Characterization of a mutant strain of Saccharomyces cerevisiae with
RT   a deletion of the RAD27 gene, a structural homolog of the RAD2
RT   nucleotide excision repair gene.";
RL   J. Bacteriol. 177:364-371(1995).
RN   [7]
RP   INTERACTION WITH POL30, AND MUTAGENESIS OF 346-PHE-PHE-347.
RX   PubMed=10899134; DOI=10.1093/emboj/19.14.3811;
RA   Gomes X.V., Burgers P.M.;
RT   "Two modes of FEN1 binding to PCNA regulated by DNA.";
RL   EMBO J. 19:3811-3821(2000).
RN   [8]
RP   FUNCTION, ENDONUCLEASE ACTIVITY, SUBSTRATE SPECIFICITY, AND
RP   MUTAGENESIS OF GLY-240.
RX   PubMed=11825897; DOI=10.1074/jbc.M110662200;
RA   Kao H.I., Henricksen L.A., Liu Y., Bambara R.A.;
RT   "Cleavage specificity of Saccharomyces cerevisiae flap endonuclease 1
RT   suggests a double-flap structure as the cellular substrate.";
RL   J. Biol. Chem. 277:14379-14389(2002).
RN   [9]
RP   FUNCTION.
RX   PubMed=12424238; DOI=10.1074/jbc.M209801200;
RA   Ayyagari R., Gomes X.V., Gordenin D.A., Burgers P.M.;
RT   "Okazaki fragment maturation in yeast. I. Distribution of functions
RT   between FEN1 AND DNA2.";
RL   J. Biol. Chem. 278:1618-1625(2003).
RN   [10]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [11]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [12]
RP   FUNCTION, AND MUTAGENESIS OF GLY-67.
RX   PubMed=16837458; DOI=10.1074/jbc.M604805200;
RA   Rossi M.L., Bambara R.A.;
RT   "Reconstituted Okazaki fragment processing indicates two pathways of
RT   primer removal.";
RL   J. Biol. Chem. 281:26051-26061(2006).
RN   [13]
RP   FUNCTION, ENDONUCLEASE AND EXONUCLEASE ACTIVITIES, AND MUTAGENESIS OF
RP   GLU-176.
RX   PubMed=17138563; DOI=10.1074/jbc.M606582200;
RA   Singh P., Zheng L., Chavez V., Qiu J., Shen B.;
RT   "Concerted action of exonuclease and Gap-dependent endonuclease
RT   activities of FEN-1 contributes to the resolution of triplet repeat
RT   sequences (CTG)n-and (GAA)n-derived secondary structures formed during
RT   maturation of Okazaki fragments.";
RL   J. Biol. Chem. 282:3465-3477(2007).
RN   [14]
RP   FUNCTION IN RDNA REPLICATION AND REPAIR.
RX   PubMed=18443037; DOI=10.1128/MCB.00200-08;
RA   Guo Z., Qian L., Liu R., Dai H., Zhou M., Zheng L., Shen B.;
RT   "Nucleolar localization and dynamic roles of flap endonuclease 1 in
RT   ribosomal DNA replication and damage repair.";
RL   Mol. Cell. Biol. 28:4310-4319(2008).
RN   [15]
RP   FUNCTION IN MITOCHONDRIAL DNA REPAIR, AND SUBCELLULAR LOCATION.
RX   PubMed=19699691; DOI=10.1016/j.dnarep.2009.07.008;
RA   Kalifa L., Beutner G., Phadnis N., Sheu S.S., Sia E.A.;
RT   "Evidence for a role of FEN1 in maintaining mitochondrial DNA
RT   integrity.";
RL   DNA Repair 8:1242-1249(2009).
RN   [16]
RP   FUNCTION IN DNA REPAIR.
RX   PubMed=19075004; DOI=10.1128/MCB.01499-08;
RA   Ma W., Panduri V., Sterling J.F., Van Houten B., Gordenin D.A.,
RA   Resnick M.A.;
RT   "The transition of closely opposed lesions to double-strand breaks
RT   during long-patch base excision repair is prevented by the coordinated
RT   action of DNA polymerase delta and Rad27/Fen1.";
RL   Mol. Cell. Biol. 29:1212-1221(2009).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Structure-specific nuclease with 5'-flap endonuclease
CC       and 5'-3' exonuclease activities involved in DNA replication and
CC       repair. During DNA replication, cleaves the 5'-overhanging flap
CC       structure that is generated by displacement synthesis when DNA
CC       polymerase encounters the 5'-end of a downstream Okazaki fragment.
CC       It enters the flap from the 5'-end and then tracks to cleave the
CC       flap base, leaving a nick for ligation. Also involved in the long
CC       patch base excision repair (LP-BER) pathway, by cleaving within
CC       the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a
CC       genome stabilization factor that prevents flaps from equilibrating
CC       into structurs that lead to duplications and deletions. Also
CC       possesses 5'-3' exonuclease activity on nicked or gapped double-
CC       stranded DNA, and exhibits RNase H activity. Also involved in
CC       replication and repair of rDNA and in repairing mitochondrial DNA.
CC       {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:11825897,
CC       ECO:0000269|PubMed:12424238, ECO:0000269|PubMed:16837458,
CC       ECO:0000269|PubMed:17138563, ECO:0000269|PubMed:18443037,
CC       ECO:0000269|PubMed:19075004, ECO:0000269|PubMed:19699691,
CC       ECO:0000269|PubMed:9166764}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03140};
CC       Note=Binds 2 magnesium ions per subunit. They probably participate
CC       in the reaction catalyzed by the enzyme. May bind an additional
CC       third magnesium ion after substrate binding. {ECO:0000255|HAMAP-
CC       Rule:MF_03140};
CC   -!- SUBUNIT: Interacts with PCNA (POL30). Three molecules of RAD27
CC       bind to one PCNA trimer with each molecule binding to one PCNA
CC       monomer. PCNA stimulates the nuclease activity without altering
CC       cleavage specificity. {ECO:0000269|PubMed:10899134}.
CC   -!- INTERACTION:
CC       P38859:DNA2; NbExp=3; IntAct=EBI-14693, EBI-5973;
CC       P15873:POL30; NbExp=3; IntAct=EBI-14693, EBI-12993;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.
CC       Mitochondrion. Note=Resides mostly in the nucleoli and relocalizes
CC       to the nucleoplasm upon DNA damage.
CC   -!- PTM: Phosphorylated. Phosphorylation upon DNA damage induces
CC       relocalization to the nuclear plasma. {ECO:0000255|HAMAP-
CC       Rule:MF_03140}.
CC   -!- MISCELLANEOUS: Present with 6120 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03140}.
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DR   EMBL; S93804; AAB21998.1; -; Genomic_DNA.
DR   EMBL; Z28113; CAA81953.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09045.1; -; Genomic_DNA.
DR   PIR; S22267; S22267.
DR   RefSeq; NP_012809.1; NM_001179679.1.
DR   ProteinModelPortal; P26793; -.
DR   SMR; P26793; 2-333.
DR   BioGrid; 34021; 372.
DR   DIP; DIP-2325N; -.
DR   IntAct; P26793; 3.
DR   MINT; MINT-536469; -.
DR   MaxQB; P26793; -.
DR   PeptideAtlas; P26793; -.
DR   EnsemblFungi; YKL113C; YKL113C; YKL113C.
DR   GeneID; 853747; -.
DR   KEGG; sce:YKL113C; -.
DR   EuPathDB; FungiDB:YKL113C; -.
DR   SGD; S000001596; RAD27.
DR   GeneTree; ENSGT00640000091478; -.
DR   InParanoid; P26793; -.
DR   KO; K04799; -.
DR   OMA; GSQDYDS; -.
DR   OrthoDB; EOG7QK0MK; -.
DR   BioCyc; YEAST:G3O-31898-MONOMER; -.
DR   Reactome; R-SCE-69166; Removal of the Flap Intermediate.
DR   NextBio; 974807; -.
DR   PRO; PR:P26793; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; IDA:SGD.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006286; P:base-excision repair, base-free sugar-phosphate removal; IMP:SGD.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IDA:SGD.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:SGD.
DR   GO; GO:0000734; P:gene conversion at mating-type locus, DNA repair synthesis; IMP:SGD.
DR   GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:GOC.
DR   GO; GO:0001302; P:replicative cell aging; IMP:SGD.
DR   Gene3D; 3.40.50.1010; -; 1.
DR   HAMAP; MF_00614; Fen; 1.
DR   InterPro; IPR020045; 5-3_exonuclease_C.
DR   InterPro; IPR023426; Flap_endonuc.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN_domain-like.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   PANTHER; PTHR11081; PTHR11081; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; SSF47807; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; DNA damage; DNA repair;
KW   DNA replication; Endonuclease; Exonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Mitochondrion; Nuclease; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1    382       Flap endonuclease 1.
FT                                /FTId=PRO_0000154038.
FT   REGION        1    105       N-domain.
FT   REGION      120    251       I-domain.
FT   REGION      339    347       Interaction with PCNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_03140}.
FT   METAL        34     34       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL        87     87       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL       156    156       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL       158    158       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL       177    177       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL       179    179       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL       231    231       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   BINDING      47     47       DNA substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   BINDING      71     71       DNA substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   BINDING     156    156       DNA substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   BINDING     229    229       DNA substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   BINDING     231    231       DNA substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   MUTAGEN      67     67       G->S: Deficient in double and single flap
FT                                endonuclease cleavage and exonucleolytic
FT                                cleavage. {ECO:0000269|PubMed:16837458}.
FT   MUTAGEN     176    176       E->A: Deficient in exonuclease and gap
FT                                endonuclease activities, but retains
FT                                almost all of its flap endonuclease
FT                                activity. {ECO:0000269|PubMed:17138563}.
FT   MUTAGEN     240    240       G->D: Can only cleave double-flap
FT                                structures with a 3' 1-nucleotide tail.
FT                                Has no exonuclease activity.
FT                                {ECO:0000269|PubMed:11825897}.
FT   MUTAGEN     346    347       FF->GA: Reduces interaction with POL30
FT                                more than 100 fold.
FT                                {ECO:0000269|PubMed:10899134}.
SQ   SEQUENCE   382 AA;  43279 MW;  1F54B08720121C8C CRC64;
     MGIKGLNAII SEHVPSAIRK SDIKSFFGRK VAIDASMSLY QFLIAVRQQD GGQLTNEAGE
     TTSHLMGMFY RTLRMIDNGI KPCYVFDGKP PDLKSHELTK RSSRRVETEK KLAEATTELE
     KMKQERRLVK VSKEHNEEAQ KLLGLMGIPY IIAPTEAEAQ CAELAKKGKV YAAASEDMDT
     LCYRTPFLLR HLTFSEAKKE PIHEIDTELV LRGLDLTIEQ FVDLCIMLGC DYCESIRGVG
     PVTALKLIKT HGSIEKIVEF IESGESNNTK WKIPEDWPYK QARMLFLDPE VIDGNEINLK
     WSPPKEKELI EYLCDDKKFS EERVKSGISR LKKGLKSGIQ GRLDGFFQVV PKTKEQLAAA
     AKRAQENKKL NKNKNKVTKG RR
//
ID   MSH3_YEAST              Reviewed;        1018 AA.
AC   P25336; D6VR92;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   11-NOV-2015, entry version 132.
DE   RecName: Full=DNA mismatch repair protein MSH3;
DE   AltName: Full=Mismatch-binding protein;
DE            Short=MBP;
DE   AltName: Full=MutS protein homolog 3;
GN   Name=MSH3; OrderedLocusNames=YCR092C; ORFNames=YCR1152, YCR92C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8510668;
RA   New L., Liu K., Crouse G.F.;
RT   "The yeast gene MSH3 defines a new class of eukaryotic MutS
RT   homologues.";
RL   Mol. Gen. Genet. 239:97-108(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1803822; DOI=10.1002/yea.320070910;
RA   Valle G., Bergantino E., Lanfranchi G., Carignani G.;
RT   "The sequence of a 6.3 kb segment of yeast chromosome III reveals an
RT   open reading frame coding for a putative mismatch binding protein.";
RL   Yeast 7:981-988(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
RA   Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
RA   Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
RA   Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
RA   Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
RA   de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
RA   Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
RA   Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
RA   Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
RA   Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
RA   Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
RA   Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
RA   Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
RA   van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
RA   Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
RA   Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   DNA-BINDING SPECIFICITY, AND INTERACTION WITH MSH2.
RX   PubMed=8805366; DOI=10.1016/S0960-9822(02)70686-6;
RA   Habraken Y., Sung P., Prakash L., Prakash S.;
RT   "Binding of insertion/deletion DNA mismatches by the heterodimer of
RT   yeast mismatch repair proteins MSH2 and MSH3.";
RL   Curr. Biol. 6:1185-1187(1996).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH MSH2.
RX   PubMed=8600025; DOI=10.1101/gad.10.4.407;
RA   Marsischky G.T., Filosi N., Kane M.F., Kolodner R.D.;
RT   "Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-
RT   dependent mismatch repair.";
RL   Genes Dev. 10:407-420(1996).
RN   [7]
RP   INTERACTION WITH POL30.
RX   PubMed=8910404; DOI=10.1074/jbc.271.45.27987;
RA   Johnson R.E., Kovvali G.K., Guzder S.N., Amin N.S., Holm C.,
RA   Habraken Y., Sung P., Prakash L., Prakash S.;
RT   "Evidence for involvement of yeast proliferating cell nuclear antigen
RT   in DNA mismatch repair.";
RL   J. Biol. Chem. 271:27987-27990(1996).
RN   [8]
RP   FUNCTION, DNA-BINDING SPECIFICITY, AND COMPLEX FORMATION WITH
RP   MLH1-PMS1.
RX   PubMed=9368761; DOI=10.1016/S0960-9822(06)00337-X;
RA   Habraken Y., Sung P., Prakash L., Prakash S.;
RT   "Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast
RT   MLH1-PMS1 complex.";
RL   Curr. Biol. 7:790-793(1997).
RN   [9]
RP   FUNCTION IN MMR.
RX   PubMed=9111357;
RA   Sia E.A., Kokoska R.J., Dominska M., Greenwell P., Petes T.D.;
RT   "Microsatellite instability in yeast: dependence on repeat unit size
RT   and DNA mismatch repair genes.";
RL   Mol. Cell. Biol. 17:2851-2858(1997).
RN   [10]
RP   FUNCTION IN NHTR.
RX   PubMed=9256462; DOI=10.1073/pnas.94.17.9214;
RA   Sugawara N., Paques F., Colaiacovo M., Haber J.E.;
RT   "Role of Saccharomyces cerevisiae Msh2 and Msh3 repair proteins in
RT   double-strand break-induced recombination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9214-9219(1997).
RN   [11]
RP   FUNCTION.
RX   PubMed=9770499; DOI=10.1073/pnas.95.21.12404;
RA   Flores-Rozas H., Kolodner R.D.;
RT   "The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent
RT   suppression of frameshift mutations.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12404-12409(1998).
RN   [12]
RP   MUTAGENESIS OF GLY-796.
RX   PubMed=10523644;
RA   Studamire B., Price G., Sugawara N., Haber J.E., Alani E.;
RT   "Separation-of-function mutations in Saccharomyces cerevisiae MSH2
RT   that confer mismatch repair defects but do not affect nonhomologous-
RT   tail removal during recombination.";
RL   Mol. Cell. Biol. 19:7558-7567(1999).
RN   [13]
RP   MUTAGENESIS OF GLN-4 AND 10-PHE-PHE-11.
RX   PubMed=11005803; DOI=10.1074/jbc.C000513200;
RA   Clark A.B., Valle F., Drotschmann K., Gary R.K., Kunkel T.A.;
RT   "Functional interaction of proliferating cell nuclear antigen with
RT   MSH2-MSH6 and MSH2-MSH3 complexes.";
RL   J. Biol. Chem. 275:36498-36501(2000).
RN   [14]
RP   IDENTIFICATION OF PROBABLE INITIATION SITE.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [15]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [16]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [17]
RP   FUNCTION.
RX   PubMed=16702432; DOI=10.1534/genetics.106.055616;
RA   Stone J.E., Petes T.D.;
RT   "Analysis of the proteins involved in the in vivo repair of base-base
RT   mismatches and four-base loops formed during meiotic recombination in
RT   the yeast Saccharomyces cerevisiae.";
RL   Genetics 173:1223-1239(2006).
RN   [18]
RP   FUNCTION IN NHTR, AND DNA-BINDING.
RX   PubMed=16781730; DOI=10.1016/j.jmb.2006.05.032;
RA   Surtees J.A., Alani E.;
RT   "Mismatch repair factor MSH2-MSH3 binds and alters the conformation of
RT   branched DNA structures predicted to form during genetic
RT   recombination.";
RL   J. Mol. Biol. 360:523-536(2006).
RN   [19]
RP   FUNCTION, DNA-BINDING, AND MUTAGENESIS OF LYS-158; LYS-160; PRO-203;
RP   GLN-226 AND ARG-247.
RX   PubMed=17157869; DOI=10.1016/j.jmb.2006.10.099;
RA   Lee S.D., Surtees J.A., Alani E.;
RT   "Saccharomyces cerevisiae MSH2-MSH3 and MSH2-MSH6 complexes display
RT   distinct requirements for DNA binding domain I in mismatch
RT   recognition.";
RL   J. Mol. Biol. 366:53-66(2007).
RN   [20]
RP   FUNCTION, AND IDENTIFICATION OF INITIATION SITE.
RX   PubMed=17636021; DOI=10.1128/MCB.00855-07;
RA   Harrington J.M., Kolodner R.D.;
RT   "Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base
RT   mispairs.";
RL   Mol. Cell. Biol. 27:6546-6554(2007).
RN   [21]
RP   FUNCTION.
RX   PubMed=17573527; DOI=10.1073/pnas.0704148104;
RA   Shell S.S., Putnam C.D., Kolodner R.D.;
RT   "Chimeric Saccharomyces cerevisiae Msh6 protein with an Msh3 mispair-
RT   binding domain combines properties of both proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10956-10961(2007).
RN   [22]
RP   INTERACTION WITH SAW1.
RX   PubMed=18471978; DOI=10.1016/j.molcel.2008.02.028;
RA   Li F., Dong J., Pan X., Oum J.-H., Boeke J.D., Lee S.E.;
RT   "Microarray-based genetic screen defines SAW1, a gene required for
RT   Rad1/Rad10-dependent processing of recombination intermediates.";
RL   Mol. Cell 30:325-335(2008).
CC   -!- FUNCTION: Component of the post-replicative DNA mismatch repair
CC       system (MMR). Heterodimerizes with MSH2 to form MutS beta, which
CC       binds to DNA mismatches thereby initiating DNA repair. MSH3
CC       provides substrate-binding and substrate specificity to the
CC       complex. When bound, the MutS beta heterodimer bends the DNA helix
CC       and shields approximately 20 base pairs. Acts mainly to repair
CC       insertion-deletion loops (IDLs) from 2 to 13 nucleotides in size,
CC       but can also repair base-base and single insertion-deletion
CC       mismatches that occur during replication. After mismatch binding,
CC       forms a ternary complex with either the MutL alpha or MutL beta
CC       heterodimer, which is thought to be responsible for directing the
CC       downstream MMR events, including strand discrimination, excision,
CC       and resynthesis. MutS beta also has a role in regulation of
CC       heteroduplex formation during mitotic and meiotic recombination.
CC       MutS beta binds to DNA flap structures predicted to form during
CC       recombination, and is required for 3' non-homologous tail removal
CC       (NHTR). MutS beta-binding alters the DNA conformation of its
CC       substrate at the ds/ssDNA junction and may facilitate its
CC       recognition and/or cleavage by the downstream nucleotide excision
CC       repair (NER) RAD1-RAD10 endonuclease. ATP binding and hydrolysis
CC       play a pivotal role in MMR and NHTR. {ECO:0000269|PubMed:16702432,
CC       ECO:0000269|PubMed:16781730, ECO:0000269|PubMed:17157869,
CC       ECO:0000269|PubMed:17573527, ECO:0000269|PubMed:17636021,
CC       ECO:0000269|PubMed:8600025, ECO:0000269|PubMed:9111357,
CC       ECO:0000269|PubMed:9256462, ECO:0000269|PubMed:9368761,
CC       ECO:0000269|PubMed:9770499}.
CC   -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC       ternary complex with either MutL alpha (MLH1-PMS1) or MutL beta
CC       (MLH1-MLH3). MutS beta interacts with proliferating cell nuclear
CC       antigen (PCNA/POL30). Interacts with SAW1.
CC       {ECO:0000269|PubMed:18471978, ECO:0000269|PubMed:8600025,
CC       ECO:0000269|PubMed:8805366, ECO:0000269|PubMed:8910404}.
CC   -!- INTERACTION:
CC       P25847:MSH2; NbExp=3; IntAct=EBI-11362, EBI-11352;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: The PIP box serves as a PCNA(POL30)-recognition and
CC       -binding motif.
CC   -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA34803.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA42247.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA46116.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X64954; CAA46116.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M96250; AAA34803.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X59720; CAA42247.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006937; DAA07561.1; -; Genomic_DNA.
DR   PIR; S19508; S19508.
DR   RefSeq; NP_010016.2; NM_001178798.1.
DR   ProteinModelPortal; P25336; -.
DR   SMR; P25336; 132-991.
DR   BioGrid; 31064; 35.
DR   DIP; DIP-2422N; -.
DR   IntAct; P25336; 24.
DR   MINT; MINT-633647; -.
DR   MaxQB; P25336; -.
DR   PeptideAtlas; P25336; -.
DR   PRIDE; P25336; -.
DR   EnsemblFungi; YCR092C; YCR092C; YCR092C.
DR   GeneID; 850454; -.
DR   KEGG; sce:YCR092C; -.
DR   EuPathDB; FungiDB:YCR092C; -.
DR   SGD; S000000688; MSH3.
DR   GeneTree; ENSGT00550000074949; -.
DR   HOGENOM; HOG000057130; -.
DR   InParanoid; P25336; -.
DR   KO; K08736; -.
DR   OMA; GYLLCIT; -.
DR   OrthoDB; EOG773XQH; -.
DR   BioCyc; YEAST:G3O-29386-MONOMER; -.
DR   Reactome; R-SCE-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   NextBio; 966078; -.
DR   PRO; PR:P25336; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   GO; GO:0032302; C:MutSbeta complex; IPI:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0032135; F:DNA insertion or deletion binding; IDA:SGD.
DR   GO; GO:0000406; F:double-strand/single-strand DNA junction binding; IDA:SGD.
DR   GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR   GO; GO:0000710; P:meiotic mismatch repair; IMP:SGD.
DR   GO; GO:0006298; P:mismatch repair; IMP:SGD.
DR   GO; GO:0006312; P:mitotic recombination; IMP:SGD.
DR   GO; GO:0000735; P:removal of nonhomologous ends; IMP:SGD.
DR   Gene3D; 3.40.1170.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR   InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01624; MutS_I; 1.
DR   Pfam; PF05188; MutS_II; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF05190; MutS_IV; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55271; SSF55271; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1   1018       DNA mismatch repair protein MSH3.
FT                                /FTId=PRO_0000115195.
FT   NP_BIND     791    798       ATP. {ECO:0000255}.
FT   REGION      126    256       Mispair-binding domain.
FT   MOTIF         4     11       PIP box.
FT   MUTAGEN       4      4       Q->A: Partially functional in a mismatch
FT                                repair assay; when associated with 10-AA-
FT                                11. {ECO:0000269|PubMed:11005803}.
FT   MUTAGEN      10     11       FF->AA: Partially functional in a
FT                                mismatch repair assay; when associated
FT                                with A-4. {ECO:0000269|PubMed:11005803}.
FT   MUTAGEN     158    158       K->A: Alters DNA-binding activity and
FT                                impairs MSH2-MSH3-mediated DNA mismatch
FT                                repair; when associated with ALA-160.
FT                                {ECO:0000269|PubMed:17157869}.
FT   MUTAGEN     160    160       K->A: Alters DNA-binding activity and
FT                                impairs MSH2-MSH3-mediated DNA mismatch
FT                                repair; when associated with ALA-158.
FT                                {ECO:0000269|PubMed:17157869}.
FT   MUTAGEN     203    203       P->A: No effect.
FT                                {ECO:0000269|PubMed:17157869}.
FT   MUTAGEN     226    226       Q->A: No effect.
FT                                {ECO:0000269|PubMed:17157869}.
FT   MUTAGEN     247    247       R->A: Impairs MSH2-MSH3-mediated DNA
FT                                mismatch repair.
FT                                {ECO:0000269|PubMed:17157869}.
FT   MUTAGEN     796    796       G->D: Defective in MMR and in NHTR.
FT                                {ECO:0000269|PubMed:10523644}.
SQ   SEQUENCE   1018 AA;  116534 MW;  1AD91C2E2F2856EF CRC64;
     MAGQPTISRF FKKAVKSELT HKQEQEVAVG NGAGSESICL DTDEEDNLSS VASTTVTNDS
     FPLKGSVSSK NSKNSEKTSG TSTTFNDIDF AKKLDRIMKR RSDENVEAED DEEEGEEDFV
     KKKARKSPTA KLTPLDKQVK DLKMHHRDKV LVIRVGYKYK CFAEDAVTVS RILHIKLVPG
     KLTIDESNPQ DCNHRQFAYC SFPDVRLNVH LERLVHHNLK VAVVEQAETS AIKKHDPGAS
     KSSVFERKIS NVFTKATFGV NSTFVLRGKR ILGDTNSIWA LSRDVHQGKV AKYSLISVNL
     NNGEVVYDEF EEPNLADEKL QIRIKYLQPI EVLVNTDDLP LHVAKFFKDI SCPLIHKQEY
     DLEDHVVQAI KVMNEKIQLS PSLIRLVSKL YSHMVEYNNE QVMLIPSIYS PFASKIHMLL
     DPNSLQSLDI FTHDGGKGSL FWLLDHTRTS FGLRMLREWI LKPLVDVHQI EERLDAIECI
     TSEINNSIFF ESLNQMLNHT PDLLRTLNRI MYGTTSRKEV YFYLKQITSF VDHFKMHQSY
     LSEHFKSSDG RIGKQSPLLF RLFSELNELL STTQLPHFLT MINVSAVMEK NSDKQVMDFF
     NLNNYDCSEG IIKIQRESES VRSQLKEELA EIRKYLKRPY LNFRDEVDYL IEVKNSQIKD
     LPDDWIKVNN TKMVSRFTTP RTQKLTQKLE YYKDLLIRES ELQYKEFLNK ITAEYTELRK
     ITLNLAQYDC ILSLAATSCN VNYVRPTFVN GQQAIIAKNA RNPIIESLDV HYVPNDIMMS
     PENGKINIIT GPNMGGKSSY IRQVALLTIM AQIGSFVPAE EIRLSIFENV LTRIGAHDDI
     INGDSTFKVE MLDILHILKN CNKRSLLLLD EVGRGTGTHD GIAISYALIK YFSELSDCPL
     ILFTTHFPML GEIKSPLIRN YHMDYVEEQK TGEDWMSVIF LYKLKKGLTY NSYGMNVAKL
     ARLDKDIINR AFSISEELRK ESINEDALKL FSSLKRILKS DNITATDKLA KLLSLDIH
//
ID   MSH6_HUMAN              Reviewed;        1360 AA.
AC   P52701; B4DF41; B4E3I4; F5H2F9; O43706; O43917; Q8TCX4; Q9BTB5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   11-NOV-2015, entry version 188.
DE   RecName: Full=DNA mismatch repair protein Msh6;
DE            Short=hMSH6;
DE   AltName: Full=G/T mismatch-binding protein;
DE            Short=GTBP;
DE            Short=GTMBP;
DE   AltName: Full=MutS-alpha 160 kDa subunit;
DE            Short=p160;
GN   Name=MSH6; Synonyms=GTBP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT GLU-39.
RX   PubMed=8942985; DOI=10.1073/pnas.93.24.13629;
RA   Acharya S., Wilson T., Gradia S., Kane M.F., Guerrette S.,
RA   Marsischky G.T., Kolodner R.D., Fishel R.;
RT   "hMSH2 forms specific mispair-binding complexes with hMSH3 and
RT   hMSH6.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:13629-13634(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   PubMed=9455487; DOI=10.1093/dnares/4.5.359;
RA   Shiwaku H.O., Wakatsuki S., Mori Y., Fukushige S., Horii A.;
RT   "Alternative splicing of GTBP in normal human tissues.";
RL   DNA Res. 4:359-362(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   TISSUE=Cerebellum, and Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-39; VAL-396;
RP   ALA-623 AND VAL-886.
RG   NIEHS SNPs program;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 69-1360, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7604265; DOI=10.1126/science.7604265;
RA   Palombo F., Gallinari P., Iaccarino I., Lettieri T., Hughes M.,
RA   D'Arrigo A., Truong O., Hsuan J.J., Jiricny J.;
RT   "GTBP, a 160-kilodalton protein essential for mismatch-binding
RT   activity in human cells.";
RL   Science 268:1912-1914(1995).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-116.
RX   PubMed=8838326; DOI=10.1006/geno.1996.0067;
RA   Nicolaides N.C., Palombo F., Kinzler K.W., Vogelstein B., Jiricny J.;
RT   "Molecular cloning of the N-terminus of GTBP.";
RL   Genomics 31:395-397(1996).
RN   [9]
RP   CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7604264; DOI=10.1126/science.7604264;
RA   Drummond J.T., Li G.-M., Longley M.J., Modrich P.;
RT   "Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch
RT   repair to tumor cells.";
RL   Science 268:1909-1912(1995).
RN   [10]
RP   FUNCTION.
RX   PubMed=9822680; DOI=10.1074/jbc.273.48.32055;
RA   Blackwell L.J., Martik D., Bjornson K.P., Bjornson E.S., Modrich P.;
RT   "Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is
RT   consistent with an ATP-dependent translocation mechanism.";
RL   J. Biol. Chem. 273:32055-32062(1998).
RN   [11]
RP   FUNCTION.
RX   PubMed=9822679; DOI=10.1074/jbc.273.48.32049;
RA   Blackwell L.J., Bjornson K.P., Modrich P.;
RT   "DNA-dependent activation of the hMutSalpha ATPase.";
RL   J. Biol. Chem. 273:32049-32054(1998).
RN   [12]
RP   FUNCTION, AND MUTAGENESIS OF LYS-1140.
RX   PubMed=9564049; DOI=10.1093/emboj/17.9.2677;
RA   Iaccarino I., Marra G., Palombo F., Jiricny J.;
RT   "hMSH2 and hMSH6 play distinct roles in mismatch binding and
RT   contribute differently to the ATPase activity of hMutSalpha.";
RL   EMBO J. 17:2677-2686(1998).
RN   [13]
RP   MISMATCH-BINDING.
RX   PubMed=9889267; DOI=10.1093/nar/27.3.736;
RA   Clark A.B., Cook M.E., Tran H.T., Gordenin D.A., Resnick M.A.,
RA   Kunkel T.A.;
RT   "Functional analysis of human MutSalpha and MutSbeta complexes in
RT   yeast.";
RL   Nucleic Acids Res. 27:736-742(1999).
RN   [14]
RP   FUNCTION.
RX   PubMed=10078208; DOI=10.1016/S1097-2765(00)80316-0;
RA   Gradia S., Subramanian D., Wilson T., Acharya S., Makhov A.,
RA   Griffith J., Fishel R.;
RT   "hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on
RT   mismatched DNA.";
RL   Mol. Cell 3:255-261(1999).
RN   [15]
RP   FUNCTION.
RX   PubMed=10660545; DOI=10.1074/jbc.275.6.3922;
RA   Gradia S., Acharya S., Fishel R.;
RT   "The role of mismatched nucleotides in activating the hMSH2-hMSH6
RT   molecular switch.";
RL   J. Biol. Chem. 275:3922-3930(2000).
RN   [16]
RP   FUNCTION.
RX   PubMed=15064730; DOI=10.1038/sj.onc.1207462;
RA   Yang Q., Zhang R., Wang X.W., Linke S.P., Sengupta S., Hickson I.D.,
RA   Pedrazzi G., Perrera C., Stagljar I., Littman S.J., Modrich P.,
RA   Harris C.C.;
RT   "The mismatch DNA repair heterodimer, hMSH2/6, regulates BLM
RT   helicase.";
RL   Oncogene 23:3749-3756(2004).
RN   [17]
RP   PHOSPHORYLATION BY PRKCZ.
RX   PubMed=15808853; DOI=10.1016/j.jmb.2005.02.001;
RA   Hernandez-Pigeon H., Quillet-Mary A., Louat T., Schambourg A.,
RA   Humbert O., Selves J., Salles B., Laurent G., Lautier D.;
RT   "hMutS alpha is protected from ubiquitin-proteasome-dependent
RT   degradation by atypical protein kinase C zeta phosphorylation.";
RL   J. Mol. Biol. 348:63-74(2005).
RN   [18]
RP   IDENTIFICATION OF MSH6 AS MEMBER OF BASC.
RX   PubMed=10783165; DOI=10.1101/gad.827000;
RA   Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.;
RT   "BASC, a super complex of BRCA1-associated proteins involved in the
RT   recognition and repair of aberrant DNA structures.";
RL   Genes Dev. 14:927-939(2000).
RN   [19]
RP   INVOLVEMENT IN HNPCC5.
RX   PubMed=9354786; DOI=10.1038/ng1197-271;
RA   Miyaki M., Konishi M., Tanaka K., Kikuchi-Yanoshita R., Muraoka M.,
RA   Yasuno M., Igari T., Koike M., Chiba M., Mori T.;
RT   "Germline mutation of MSH6 as the cause of hereditary nonpolyposis
RT   colorectal cancer.";
RL   Nat. Genet. 17:271-272(1997).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-227 AND
RP   SER-261, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-41 AND SER-43,
RP   VARIANT [LARGE SCALE ANALYSIS] GLU-39, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [22]
RP   INVOLVEMENT IN MMRCS.
RX   PubMed=17557300; DOI=10.1002/humu.20569;
RA   Auclair J., Leroux D., Desseigne F., Lasset C., Saurin J.C.,
RA   Joly M.O., Pinson S., Xu X.L., Montmain G., Ruano E., Navarro C.,
RA   Puisieux A., Wang Q.;
RT   "Novel biallelic mutations in MSH6 and PMS2 genes: gene conversion as
RT   a likely cause of PMS2 gene inactivation.";
RL   Hum. Mutat. 28:1084-1090(2007).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-79; SER-91;
RP   SER-137; SER-200; SER-227; SER-252; SER-254; SER-256 AND SER-261, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [27]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-504, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-137; SER-227 AND
RP   SER-830, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [29]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [30]
RP   INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL12.
RX   PubMed=21957315; DOI=10.1128/JVI.05487-11;
RA   Mohni K.N., Mastrocola A.S., Bai P., Weller S.K., Heinen C.D.;
RT   "DNA mismatch repair proteins are required for efficient herpes
RT   simplex virus 1 replication.";
RL   J. Virol. 85:12241-12253(2011).
RN   [31]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-137; SER-219;
RP   SER-227; SER-252; SER-261; THR-269; SER-274; SER-275; SER-279; SER-280
RP   AND SER-309, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [32]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-103 AND
RP   105-TRP-TRP-106.
RX   PubMed=23622243; DOI=10.1016/j.cell.2013.03.025;
RA   Li F., Mao G., Tong D., Huang J., Gu L., Yang W., Li G.M.;
RT   "The histone mark H3K36me3 regulates human DNA mismatch repair through
RT   its interaction with MutSalpha.";
RL   Cell 153:590-600(2013).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
RX   PubMed=17531815; DOI=10.1016/j.molcel.2007.04.018;
RA   Warren J.J., Pohlhaus T.J., Changela A., Iyer R.R., Modrich P.L.,
RA   Beese L.S.;
RT   "Structure of the human MutSalpha DNA lesion recognition complex.";
RL   Mol. Cell 26:579-592(2007).
RN   [34]
RP   VARIANTS VAL-1213 AND ILE-1260.
RX   PubMed=7604266; DOI=10.1126/science.7604266;
RA   Papadopoulos N., Nicolaides N.C., Liu B., Parsons R., Lengauer C.,
RA   Palombo F., D'Arrigo A., Markowitz S., Willson J.K.V., Kinzler K.W.,
RA   Jiricny J., Vogelstein B.;
RT   "Mutations of GTBP in genetically unstable cells.";
RL   Science 268:1915-1917(1995).
RN   [35]
RP   VARIANTS HNPCC5 ILE-144 AND CYS-850.
RX   PubMed=10521294; DOI=10.1086/302612;
RA   Wu Y., Berends M.J.W., Mensink R.G.J., Kempinga C., Sijmons R.H.,
RA   van Der Zee A.G.J., Hollema H., Kleibeuker J.H., Buys C.H.C.M.,
RA   Hofstra R.M.W.;
RT   "Association of hereditary nonpolyposis colorectal cancer-related
RT   tumors displaying low microsatellite instability with MSH6 germline
RT   mutations.";
RL   Am. J. Hum. Genet. 65:1291-1298(1999).
RN   [36]
RP   VARIANTS CRC ILE-285; ARG-566; GLY-803 AND THR-1087, AND VARIANTS
RP   GLU-39; ASP-220; VAL-396 AND LEU-800.
RX   PubMed=10537275;
RA   Kolodner R.D., Tytell J.D., Schmeits J.L., Kane M.F., Das Gupta R.,
RA   Weger J., Wahlberg S., Fox E.A., Peel D., Ziogas A., Garber J.E.,
RA   Syngal S., Anton-Culver H., Li F.P.;
RT   "Germ-line msh6 mutations in colorectal cancer families.";
RL   Cancer Res. 59:5068-5074(1999).
RN   [37]
RP   VARIANT HNPCC5 GLU-698.
RX   PubMed=10480359; DOI=10.1007/s004399900064;
RA   Wang Q., Lasset C., Desseigne F., Saurin J.-C., Maugard C.,
RA   Navarro C., Ruano E., Descos L., Trillet-Lenoir V., Bosset J.-F.,
RA   Puisieux A.;
RT   "Prevalence of germline mutations of hMLH1, hMSH2, hPMS1, hPMS2, and
RT   hMSH6 genes in 75 French kindreds with nonpolyposis colorectal
RT   cancer.";
RL   Hum. Genet. 105:79-85(1999).
RN   [38]
RP   VARIANT CRC MET-1284.
RX   PubMed=10413423; DOI=10.1093/jnci/91.14.1221;
RA   Chan T.L., Yuen S.T., Chung L.P., Ho J.W.C., Kwan K.Y.M., Chan A.S.Y.,
RA   Ho J.C.Y., Leung S.Y., Wyllie A.H.;
RT   "Frequent microsatellite instability and mismatch repair gene
RT   mutations in young Chinese patients with colorectal cancer.";
RL   J. Natl. Cancer Inst. 91:1221-1226(1999).
RN   [39]
RP   VARIANTS COLORECTAL/ENDOMETRIAL CANCER VAL-20; ALA-878 AND HIS-901.
RX   PubMed=11153917; DOI=10.1007/s004390000417;
RA   Charames G.S., Millar A.L., Pal T., Narod S., Bapat B.;
RT   "Do MSH6 mutations contribute to double primary cancers of the
RT   colorectum and endometrium?";
RL   Hum. Genet. 107:623-629(2000).
RN   [40]
RP   VARIANT CRC SER-340, AND VARIANT GLU-39.
RX   PubMed=10699937;
RX   DOI=10.1002/(SICI)1097-0215(20000301)85:5<606::AID-IJC2>3.0.CO;2-B;
RA   Plaschke J., Kruppa C., Tischler R., Bocker T., Pistorius S.,
RA   Dralle H., Rueschoff J., Saeger H.D., Fishel R., Schackert H.K.;
RT   "Sequence analysis of the mismatch repair gene hMSH6 in the germline
RT   of patients with familial and sporadic colorectal cancer.";
RL   Int. J. Cancer 85:606-613(2000).
RN   [41]
RP   VARIANTS CRC ALA-685; GLN-772; ALA-800; MET-854; ALA-878; VAL-1031 AND
RP   ARG-1158.
RX   PubMed=11470537; DOI=10.1016/S0378-1119(01)00517-0;
RA   Ohmiya N., Matsumoto S., Yamamoto H., Baranovskaya S.,
RA   Malkhosyan S.R., Perucho M.;
RT   "Germline and somatic mutations in hMSH6 and hMSH3 in gastrointestinal
RT   cancers of the microsatellite mutator phenotype.";
RL   Gene 272:301-313(2001).
RN   [42]
RP   VARIANT HNPCC5 ALA-878.
RX   PubMed=11586295; DOI=10.1038/ng1001-137;
RA   Wu Y., Berends M.J.W., Sijmons R.H., Mensink R.G.J., Verlind E.,
RA   Kooi K.A., van der Sluis T., Kempinga C., van der Zee A.G.J.,
RA   Hollema H., Buys C.H.C.M., Kleibeuker J.H., Hofstra R.M.W.;
RT   "A role for MLH3 in hereditary nonpolyposis colorectal cancer.";
RL   Nat. Genet. 29:137-138(2001).
RN   [43]
RP   VARIANTS CRC ILE-144; ARG-522; MET-725; CYS-850; ALA-878; ASP-1021;
RP   MET-1100; ILE-1219 AND ASP-1248.
RX   PubMed=11709755; DOI=10.1086/337944;
RA   Berends M.J.W., Wu Y., Sijmons R.H., Mensink R.G.J., van der Sluis T.,
RA   Hordijk-Hos J.M., de Vries E.G.E., Hollema H., Karrenbeld A.,
RA   Buys C.H.C.M., van der Zee A.G.J., Hofstra R.M.W., Kleibeuker J.H.;
RT   "Molecular and clinical characteristics of MSH6 variants: an analysis
RT   of 25 index carriers of a germline variant.";
RL   Am. J. Hum. Genet. 70:26-37(2002).
RN   [44]
RP   VARIANT CRC HIS-976.
RX   PubMed=11807791; DOI=10.1002/ijc.10097;
RA   Plaschke J., Krueger S., Pistorius S., Theissig F., Saeger H.D.,
RA   Schackert H.K.;
RT   "Involvement of hMSH6 in the development of hereditary and sporadic
RT   colorectal cancer revealed by immunostaining is based on germline
RT   mutations, but rarely on somatic inactivation.";
RL   Int. J. Cancer 97:643-648(2002).
RN   [45]
RP   VARIANT HNPCC5 VAL-492.
RX   PubMed=12658575; DOI=10.1086/373963;
RA   Wagner A., Barrows A., Wijnen J.T., van der Klift H., Franken P.F.,
RA   Verkuijlen P., Nakagawa H., Geugien M., Jaghmohan-Changur S.,
RA   Breukel C., Meijers-Heijboer H., Morreau H., van Puijenbroek M.,
RA   Burn J., Coronel S., Kinarski Y., Okimoto R., Watson P., Lynch J.F.,
RA   de la Chapelle A., Lynch H.T., Fodde R.;
RT   "Molecular analysis of hereditary nonpolyposis colorectal cancer in
RT   the United States: high mutation detection rate among clinically
RT   selected families and characterization of an American founder genomic
RT   deletion of the MSH2 gene.";
RL   Am. J. Hum. Genet. 72:1088-1100(2003).
RN   [46]
RP   VARIANTS CRC HIS-1095 AND GLN-1354.
RX   PubMed=12522549; DOI=10.1007/s00439-002-0866-4;
RA   Kariola R., Otway R., Loennqvist K.E., Raevaara T.E., Macrae F.,
RA   Vos Y.J., Kohonen-Corish M., Hofstra R.M.W., Nystroem-Lahti M.;
RT   "Two mismatch repair gene mutations found in a colon cancer patient -
RT   which one is pathogenic?";
RL   Hum. Genet. 112:105-109(2003).
RN   [47]
RP   VARIANT CRC ALA-54, AND VARIANTS GLU-39; ALA-509; MET-854 AND ALA-878.
RX   PubMed=14520694; DOI=10.1002/ijc.11415;
RA   Peterlongo P., Nafa K., Lerman G.S., Glogowski E., Shia J., Ye T.Z.,
RA   Markowitz A.J., Guillem J.G., Kolachana P., Boyd J.A., Offit K.,
RA   Ellis N.A.;
RT   "MSH6 germline mutations are rare in colorectal cancer families.";
RL   Int. J. Cancer 107:571-579(2003).
RN   [48]
RP   VARIANTS LEU-128; LEU-623; THR-728 AND LYS-1193, AND CHARACTERIZATION
RP   OF VARIANTS LEU-128; LEU-623; THR-728 AND LYS-1193.
RX   PubMed=15354210; DOI=10.1038/sj.bjc.6602129;
RA   Kariola R., Hampel H., Frankel W.L., Raevaara T.E., de la Chapelle A.,
RA   Nystroem-Lahti M.;
RT   "MSH6 missense mutations are often associated with no or low cancer
RT   susceptibility.";
RL   Br. J. Cancer 91:1287-1292(2004).
RN   [49]
RP   VARIANT HNPCC5 TRP-772.
RX   PubMed=14974087; DOI=10.1002/humu.9217;
RG   The German HNPCC consortium;
RA   Plaschke J., Krueger S., Dietmaier W., Gebert J., Sutter C.,
RA   Mangold E., Pagenstecher C., Holinski-Feder E., Schulmann K.,
RA   Moeslein G., Rueschoff J., Engel C., Evans G., Schackert H.K.;
RT   "Eight novel MSH6 germline mutations in patients with familial and
RT   nonfamilial colorectal cancer selected by loss of protein expression
RT   in tumor tissue.";
RL   Hum. Mutat. 23:285-285(2004).
RN   [50]
RP   VARIANT HNPCC5 VAL-1163.
RX   PubMed=15365995; DOI=10.1002/humu.9277;
RA   Shin Y.-K., Heo S.-C., Shin J.-H., Hong S.-H., Ku J.-L., Yoo B.-C.,
RA   Kim I.-J., Park J.-G.;
RT   "Germline mutations in MLH1, MSH2 and MSH6 in Korean hereditary non-
RT   polyposis colorectal cancer families.";
RL   Hum. Mutat. 24:351-351(2004).
RN   [51]
RP   VARIANT COLORECTAL/ENDOMETRIAL CANCER PRO-449.
RX   PubMed=14961575; DOI=10.1002/ijc.11718;
RA   Cederquist K., Emanuelsson M., Goeransson I., Holinski-Feder E.,
RA   Mueller-Koch Y., Golovleva I., Groenberg H.;
RT   "Mutation analysis of the MLH1, MSH2 and MSH6 genes in patients with
RT   double primary cancers of the colorectum and the endometrium: a
RT   population-based study in northern Sweden.";
RL   Int. J. Cancer 109:370-376(2004).
RN   [52]
RP   VARIANTS CRC ASN-99; ASP-619; VAL-787; ALA-878 AND CYS-1076.
RX   PubMed=15483016; DOI=10.1200/JCO.2004.02.033;
RA   Plaschke J., Engel C., Krueger S., Holinski-Feder E., Pagenstecher C.,
RA   Mangold E., Moeslein G., Schulmann K., Gebert J.,
RA   von Knebel Doeberitz M., Rueschoff J., Loeffler M., Schackert H.K.;
RT   "Lower incidence of colorectal cancer and later age of disease onset
RT   in 27 families with pathogenic MSH6 germline mutations compared with
RT   families with MLH1 or MSH2 mutations: the German hereditary
RT   nonpolyposis colorectal cancer consortium.";
RL   J. Clin. Oncol. 22:4486-4494(2004).
RN   [53]
RP   VARIANTS [LARGE SCALE ANALYSIS] ASP-221 AND VAL-492.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [54]
RP   VARIANTS THR-13; LEU-65; ILE-144; HIS-468; CYS-503; LEU-580; ALA-878;
RP   LEU-1232 AND GLY-1321.
RX   PubMed=18033691; DOI=10.1002/humu.20635;
RA   Barnetson R.A., Cartwright N., van Vliet A., Haq N., Drew K.,
RA   Farrington S., Williams N., Warner J., Campbell H., Porteous M.E.,
RA   Dunlop M.G.;
RT   "Classification of ambiguous mutations in DNA mismatch repair genes
RT   identified in a population-based study of colorectal cancer.";
RL   Hum. Mutat. 29:367-374(2008).
RN   [55]
RP   CHARACTERIZATION OF VARIANT HNPCC5 VAL-20, CHARACTERIZATION OF
RP   VARIANTS CRC HIS-976 AND ASP-1021, AND CHARACTERIZATION OF VARIANTS
RP   SER-25; VAL-326; VAL-396; VAL-492; CYS-503; ARG-522; ASN-610; CYS-850;
RP   ALA-878; TYR-1026; SER-1087 AND MET-1225.
RX   PubMed=22102614; DOI=10.1002/humu.22000;
RA   Drost M., Zonneveld J.B., van Hees S., Rasmussen L.J., Hofstra R.M.,
RA   de Wind N.;
RT   "A rapid and cell-free assay to test the activity of lynch syndrome-
RT   associated MSH2 and MSH6 missense variants.";
RL   Hum. Mutat. 33:488-494(2012).
RN   [56]
RP   CHARACTERIZATION OF VARIANTS PRO-435; PRO-585; THR-677; ALA-878;
RP   HIS-1095 AND GLN-1354.
RX   PubMed=22581703; DOI=10.1002/humu.22119;
RA   Kantelinen J., Kansikas M., Candelin S., Hampel H., Smith B., Holm L.,
RA   Kariola R., Nystrom M.;
RT   "Mismatch repair analysis of inherited MSH2 and/or MSH6 variation
RT   pairs found in cancer patients.";
RL   Hum. Mutat. 33:1294-1301(2012).
CC   -!- FUNCTION: Component of the post-replicative DNA mismatch repair
CC       system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which
CC       binds to DNA mismatches thereby initiating DNA repair. When bound,
CC       MutS alpha bends the DNA helix and shields approximately 20 base
CC       pairs, and recognizes single base mismatches and dinucleotide
CC       insertion-deletion loops (IDL) in the DNA. After mismatch binding,
CC       forms a ternary complex with the MutL alpha heterodimer, which is
CC       thought to be responsible for directing the downstream MMR events,
CC       including strand discrimination, excision, and resynthesis. ATP
CC       binding and hydrolysis play a pivotal role in mismatch repair
CC       functions. The ATPase activity associated with MutS alpha
CC       regulates binding similar to a molecular switch: mismatched DNA
CC       provokes ADP-->ATP exchange, resulting in a discernible
CC       conformational transition that converts MutS alpha into a sliding
CC       clamp capable of hydrolysis-independent diffusion along the DNA
CC       backbone. This transition is crucial for mismatch repair. MutS
CC       alpha may also play a role in DNA homologous recombination repair.
CC       Recruited on chromatin in G1 and early S phase via its PWWP domain
CC       that specifically binds trimethylated 'Lys-36' of histone H3
CC       (H3K36me3): early recruitment to chromatin to be replicated
CC       allowing a quick identification of mismatch repair to initiate the
CC       DNA mismatch repair reaction. {ECO:0000269|PubMed:10078208,
CC       ECO:0000269|PubMed:10660545, ECO:0000269|PubMed:15064730,
CC       ECO:0000269|PubMed:23622243, ECO:0000269|PubMed:9564049,
CC       ECO:0000269|PubMed:9822679, ECO:0000269|PubMed:9822680}.
CC   -!- SUBUNIT: Heterodimer consisting of MSH2-MSH6 (MutS alpha). Forms a
CC       ternary complex with MutL alpha (MLH1-PMS1). Interacts with EXO1.
CC       Part of the BRCA1-associated genome surveillance complex (BASC),
CC       which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the
CC       RAD50-MRE11-NBS1 protein complex. This association could be a
CC       dynamic process changing throughout the cell cycle and within
CC       subnuclear domains. Interacts with ATR. Interacts with herpes
CC       simplex virus 1 protein UL12 (PubMed:21957315).
CC       {ECO:0000269|PubMed:21957315}.
CC   -!- INTERACTION:
CC       P43246:MSH2; NbExp=5; IntAct=EBI-395529, EBI-355888;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23622243}.
CC       Chromosome {ECO:0000269|PubMed:23622243}. Note=Associates with
CC       H3K36me3 via its PWWP domain.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=GTBP-N;
CC         IsoId=P52701-1; Sequence=Displayed;
CC       Name=GTBP-alt;
CC         IsoId=P52701-2; Sequence=VSP_003291, VSP_003292;
CC       Name=3;
CC         IsoId=P52701-3; Sequence=VSP_054419;
CC         Note=No experimental confirmation available.;
CC       Name=4;
CC         IsoId=P52701-4; Sequence=VSP_055020;
CC         Note=No experimental confirmation available.;
CC   -!- DOMAIN: The PWWP domain specifically recognizes and binds
CC       trimethylated 'Lys-36' of histone H3 (H3K36me3).
CC       {ECO:0000269|PubMed:23622243}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Phosphorylated by PRKCZ, which may prevent MutS alpha
CC       degradation by the ubiquitin-proteasome pathway.
CC       {ECO:0000269|PubMed:15808853}.
CC   -!- DISEASE: Hereditary non-polyposis colorectal cancer 5 (HNPCC5)
CC       [MIM:614350]: An autosomal dominant disease associated with marked
CC       increase in cancer susceptibility. It is characterized by a
CC       familial predisposition to early-onset colorectal carcinoma (CRC)
CC       and extra-colonic tumors of the gastrointestinal, urological and
CC       female reproductive tracts. HNPCC is reported to be the most
CC       common form of inherited colorectal cancer in the Western world.
CC       Clinically, HNPCC is often divided into two subgroups. Type I is
CC       characterized by hereditary predisposition to colorectal cancer, a
CC       young age of onset, and carcinoma observed in the proximal colon.
CC       Type II is characterized by increased risk for cancers in certain
CC       tissues such as the uterus, ovary, breast, stomach, small
CC       intestine, skin, and larynx in addition to the colon. Diagnosis of
CC       classical HNPCC is based on the Amsterdam criteria: 3 or more
CC       relatives affected by colorectal cancer, one a first degree
CC       relative of the other two; 2 or more generation affected; 1 or
CC       more colorectal cancers presenting before 50 years of age;
CC       exclusion of hereditary polyposis syndromes. The term 'suspected
CC       HNPCC' or 'incomplete HNPCC' can be used to describe families who
CC       do not or only partially fulfill the Amsterdam criteria, but in
CC       whom a genetic basis for colon cancer is strongly suspected.
CC       {ECO:0000269|PubMed:10480359, ECO:0000269|PubMed:10521294,
CC       ECO:0000269|PubMed:11586295, ECO:0000269|PubMed:12658575,
CC       ECO:0000269|PubMed:14974087, ECO:0000269|PubMed:15365995,
CC       ECO:0000269|PubMed:9354786}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of
CC       endometrium, the mucous lining of the uterus. Most endometrial
CC       cancers are adenocarcinomas, cancers that begin in cells that make
CC       and release mucus and other fluids. {ECO:0000269|PubMed:11153917,
CC       ECO:0000269|PubMed:14961575}. Note=Disease susceptibility is
CC       associated with variations affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: An
CC       autosomal recessive, rare, childhood cancer predisposition
CC       syndrome encompassing a broad tumor spectrum. This includes
CC       hematological malignancies, central nervous system tumors, Lynch
CC       syndrome-associated malignancies such as colorectal tumors as well
CC       as multiple intestinal polyps, embryonic tumors and
CC       rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature
CC       reminiscent of neurofibromatosis type 1, are often found as first
CC       manifestation of the underlying cancer. Areas of skin
CC       hypopigmentation have also been reported in MMRCS patients.
CC       {ECO:0000269|PubMed:17557300}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PWWP domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00162}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/MSH6ID344ch2p16.html";
CC   -!- WEB RESOURCE: Name=Hereditary non-polyposis colorectal cancer db;
CC       URL="http://www.nfdht.nl/";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/msh6/";
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DR   EMBL; U73737; AAB47425.1; -; Genomic_DNA.
DR   EMBL; U73732; AAB47425.1; JOINED; Genomic_DNA.
DR   EMBL; U73733; AAB47425.1; JOINED; Genomic_DNA.
DR   EMBL; U73734; AAB47425.1; JOINED; Genomic_DNA.
DR   EMBL; U73736; AAB47425.1; JOINED; Genomic_DNA.
DR   EMBL; D89645; BAA23674.1; -; Genomic_DNA.
DR   EMBL; D89646; BAA23675.1; -; mRNA.
DR   EMBL; AK293921; BAG57302.1; -; mRNA.
DR   EMBL; AK304735; BAG65496.1; -; mRNA.
DR   EMBL; AY082894; AAL87401.1; -; Genomic_DNA.
DR   EMBL; AC006509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004246; AAH04246.1; -; mRNA.
DR   EMBL; U54777; AAB39212.2; -; mRNA.
DR   EMBL; U28946; AAC50461.1; -; mRNA.
DR   CCDS; CCDS1836.1; -. [P52701-1]
DR   CCDS; CCDS62906.1; -. [P52701-3]
DR   CCDS; CCDS62907.1; -. [P52701-4]
DR   PIR; JC5839; JC5839.
DR   RefSeq; NP_000170.1; NM_000179.2. [P52701-1]
DR   RefSeq; NP_001268421.1; NM_001281492.1. [P52701-3]
DR   RefSeq; NP_001268422.1; NM_001281493.1. [P52701-4]
DR   RefSeq; NP_001268423.1; NM_001281494.1. [P52701-4]
DR   UniGene; Hs.445052; -.
DR   PDB; 2GFU; NMR; -; A=68-201.
DR   PDB; 2O8B; X-ray; 2.75 A; B=341-1360.
DR   PDB; 2O8C; X-ray; 3.37 A; B=341-1360.
DR   PDB; 2O8D; X-ray; 3.00 A; B=341-1360.
DR   PDB; 2O8E; X-ray; 3.30 A; B=341-1360.
DR   PDB; 2O8F; X-ray; 3.25 A; B=341-1360.
DR   PDBsum; 2GFU; -.
DR   PDBsum; 2O8B; -.
DR   PDBsum; 2O8C; -.
DR   PDBsum; 2O8D; -.
DR   PDBsum; 2O8E; -.
DR   PDBsum; 2O8F; -.
DR   ProteinModelPortal; P52701; -.
DR   SMR; P52701; 68-201, 362-1335.
DR   BioGrid; 109211; 54.
DR   DIP; DIP-32972N; -.
DR   IntAct; P52701; 24.
DR   MINT; MINT-131993; -.
DR   STRING; 9606.ENSP00000234420; -.
DR   PhosphoSite; P52701; -.
DR   BioMuta; MSH6; -.
DR   DMDM; 68067672; -.
DR   MaxQB; P52701; -.
DR   PaxDb; P52701; -.
DR   PeptideAtlas; P52701; -.
DR   PRIDE; P52701; -.
DR   DNASU; 2956; -.
DR   Ensembl; ENST00000234420; ENSP00000234420; ENSG00000116062. [P52701-1]
DR   Ensembl; ENST00000538136; ENSP00000438580; ENSG00000116062. [P52701-4]
DR   Ensembl; ENST00000540021; ENSP00000446475; ENSG00000116062. [P52701-3]
DR   Ensembl; ENST00000614496; ENSP00000477844; ENSG00000116062. [P52701-4]
DR   GeneID; 2956; -.
DR   KEGG; hsa:2956; -.
DR   UCSC; uc002rwc.2; human. [P52701-2]
DR   UCSC; uc002rwd.4; human. [P52701-1]
DR   CTD; 2956; -.
DR   GeneCards; MSH6; -.
DR   GeneReviews; MSH6; -.
DR   HGNC; HGNC:7329; MSH6.
DR   HPA; CAB009091; -.
DR   HPA; HPA028376; -.
DR   HPA; HPA028446; -.
DR   MIM; 276300; phenotype.
DR   MIM; 600678; gene.
DR   MIM; 608089; phenotype.
DR   MIM; 614350; phenotype.
DR   neXtProt; NX_P52701; -.
DR   Orphanet; 252202; Constitutional mismatch repair deficiency syndrome.
DR   Orphanet; 144; Hereditary nonpolyposis colon cancer.
DR   Orphanet; 587; Muir-Torre syndrome.
DR   Orphanet; 99817; Non-polyposis Turcot syndrome.
DR   PharmGKB; PA184; -.
DR   eggNOG; KOG0217; Eukaryota.
DR   eggNOG; COG0249; LUCA.
DR   GeneTree; ENSGT00550000075024; -.
DR   HOGENOM; HOG000243127; -.
DR   HOVERGEN; HBG000101; -.
DR   InParanoid; P52701; -.
DR   KO; K08737; -.
DR   OMA; ALKDCMR; -.
DR   OrthoDB; EOG7K9K27; -.
DR   PhylomeDB; P52701; -.
DR   TreeFam; TF105842; -.
DR   Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   ChiTaRS; MSH6; human.
DR   EvolutionaryTrace; P52701; -.
DR   GeneWiki; MSH6; -.
DR   GenomeRNAi; 2956; -.
DR   NextBio; 11716; -.
DR   PMAP-CutDB; P52701; -.
DR   PRO; PR:P52701; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; P52701; -.
DR   CleanEx; HS_MSH6; -.
DR   ExpressionAtlas; P52701; baseline and differential.
DR   Genevisible; P52701; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0032301; C:MutSalpha complex; IDA:UniProtKB.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
DR   GO; GO:0000228; C:nuclear chromosome; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
DR   GO; GO:0032137; F:guanine/thymine mispair binding; IEA:Ensembl.
DR   GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR   GO; GO:0030983; F:mismatched DNA binding; IDA:UniProtKB.
DR   GO; GO:0008340; P:determination of adult lifespan; ISS:BHF-UCL.
DR   GO; GO:0006281; P:DNA repair; IDA:BHF-UCL.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISS:BHF-UCL.
DR   GO; GO:0045190; P:isotype switching; ISS:BHF-UCL.
DR   GO; GO:0000710; P:meiotic mismatch repair; ISS:BHF-UCL.
DR   GO; GO:0006298; P:mismatch repair; IDA:UniProtKB.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IDA:BHF-UCL.
DR   GO; GO:0051096; P:positive regulation of helicase activity; IDA:BHF-UCL.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR   GO; GO:0009411; P:response to UV; ISS:BHF-UCL.
DR   GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; ISS:BHF-UCL.
DR   GO; GO:0016447; P:somatic recombination of immunoglobulin gene segments; ISS:BHF-UCL.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1170.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR   InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000313; PWWP_dom.
DR   Pfam; PF01624; MutS_I; 1.
DR   Pfam; PF05188; MutS_II; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF05190; MutS_IV; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55271; SSF55271; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   PROSITE; PS50812; PWWP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Chromosome; Complete proteome; Direct protein sequencing;
KW   Disease mutation; DNA damage; DNA repair; DNA-binding;
KW   Hereditary nonpolyposis colorectal cancer; Host-virus interaction;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome.
FT   CHAIN         1   1360       DNA mismatch repair protein Msh6.
FT                                /FTId=PRO_0000115207.
FT   DOMAIN       92    154       PWWP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   NP_BIND    1134   1141       ATP. {ECO:0000255}.
FT   COMPBIAS     34     37       Poly-Ala.
FT   COMPBIAS    201    209       Poly-Glu.
FT   COMPBIAS   1118   1123       Poly-Glu.
FT   MOD_RES      14     14       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES      41     41       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243}.
FT   MOD_RES      43     43       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243}.
FT   MOD_RES      70     70       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES      79     79       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES      91     91       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     137    137       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     200    200       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     219    219       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     227    227       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     252    252       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     254    254       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     256    256       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     261    261       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     269    269       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     274    274       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     275    275       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     279    279       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     280    280       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     309    309       Phosphoserine.
FT                                {ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     504    504       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     830    830       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   VAR_SEQ       1    302       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_055020.
FT   VAR_SEQ      80    209       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054419.
FT   VAR_SEQ    1058   1068       DVLLCLANYSR -> GKTLNKLVLRL (in isoform
FT                                GTBP-alt). {ECO:0000305}.
FT                                /FTId=VSP_003291.
FT   VAR_SEQ    1069   1360       Missing (in isoform GTBP-alt).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_003292.
FT   VARIANT      13     13       K -> T (in dbSNP:rs41294988).
FT                                {ECO:0000269|PubMed:18033691}.
FT                                /FTId=VAR_038032.
FT   VARIANT      20     20       A -> V (in colorectal/endometrial cancer
FT                                and HNPCC5; repair proficient;
FT                                dbSNP:rs63750664).
FT                                {ECO:0000269|PubMed:11153917,
FT                                ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_043943.
FT   VARIANT      25     25       A -> S (associated with HNPCC5; unknown
FT                                pathologiacl significance; repair
FT                                proficient).
FT                                {ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_067294.
FT   VARIANT      25     25       A -> V (in dbSNP:rs35462442).
FT                                /FTId=VAR_038033.
FT   VARIANT      39     39       G -> E (in dbSNP:rs1042821).
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000269|PubMed:10537275,
FT                                ECO:0000269|PubMed:10699937,
FT                                ECO:0000269|PubMed:14520694,
FT                                ECO:0000269|PubMed:8942985,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_004490.
FT   VARIANT      54     54       G -> A (in CRC; unknown pathological
FT                                significance; dbSNP:rs63751098).
FT                                {ECO:0000269|PubMed:14520694}.
FT                                /FTId=VAR_043944.
FT   VARIANT      65     65       S -> L (in dbSNP:rs41294984).
FT                                {ECO:0000269|PubMed:18033691}.
FT                                /FTId=VAR_038034.
FT   VARIANT      99     99       K -> N (in CRC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:15483016}.
FT                                /FTId=VAR_043945.
FT   VARIANT     128    128       R -> L (no impairment of
FT                                heterodimerization with MSH2 and of in
FT                                vitro mismatch repair capacity).
FT                                {ECO:0000269|PubMed:15354210}.
FT                                /FTId=VAR_043946.
FT   VARIANT     144    144       S -> I (in suspected HNPCC5 and CRC;
FT                                dbSNP:rs3211299).
FT                                {ECO:0000269|PubMed:10521294,
FT                                ECO:0000269|PubMed:11709755,
FT                                ECO:0000269|PubMed:18033691}.
FT                                /FTId=VAR_012955.
FT   VARIANT     220    220       E -> D (in dbSNP:rs1800938).
FT                                {ECO:0000269|PubMed:10537275}.
FT                                /FTId=VAR_012956.
FT   VARIANT     221    221       E -> D (in dbSNP:rs41557217).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_042274.
FT   VARIANT     285    285       S -> I (in CRC).
FT                                {ECO:0000269|PubMed:10537275}.
FT                                /FTId=VAR_012957.
FT   VARIANT     295    295       K -> R (in multiple colorectal adenoma).
FT                                /FTId=VAR_043947.
FT   VARIANT     326    326       A -> V (associated with HNPCC5; unknown
FT                                pathological significance; repair
FT                                proficient).
FT                                {ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_067295.
FT   VARIANT     340    340       F -> S (in CRC, breast cancer and
FT                                leukemia). {ECO:0000269|PubMed:10699937}.
FT                                /FTId=VAR_043948.
FT   VARIANT     396    396       L -> V (associated with HNPCC5; unknown
FT                                pathological significance; repair
FT                                proficient; dbSNP:rs2020908).
FT                                {ECO:0000269|PubMed:10537275,
FT                                ECO:0000269|PubMed:22102614,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_012958.
FT   VARIANT     435    435       L -> P (mismatch repair deficient).
FT                                {ECO:0000269|PubMed:22581703}.
FT                                /FTId=VAR_068710.
FT   VARIANT     449    449       L -> P (in colorectal/endometrial cancer;
FT                                unknown pathological significance).
FT                                {ECO:0000269|PubMed:14961575}.
FT                                /FTId=VAR_043949.
FT   VARIANT     468    468       R -> H (in dbSNP:rs41295268).
FT                                {ECO:0000269|PubMed:18033691}.
FT                                /FTId=VAR_038035.
FT   VARIANT     492    492       M -> V (associated with HNPCC5; unknown
FT                                pathological significance; repair
FT                                proficient).
FT                                {ECO:0000269|PubMed:12658575,
FT                                ECO:0000269|PubMed:17344846,
FT                                ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_042275.
FT   VARIANT     503    503       S -> C (associated with HNPCC5; unknown
FT                                pathological significance; repair
FT                                proficient).
FT                                {ECO:0000269|PubMed:18033691,
FT                                ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_038036.
FT   VARIANT     509    509       V -> A. {ECO:0000269|PubMed:14520694}.
FT                                /FTId=VAR_043950.
FT   VARIANT     522    522       Q -> R (in CRC; also associated with
FT                                HNPCC5; repair proficient).
FT                                {ECO:0000269|PubMed:11709755,
FT                                ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_043951.
FT   VARIANT     538    538       Y -> S (in dbSNP:rs728619).
FT                                /FTId=VAR_038037.
FT   VARIANT     566    566       G -> R (in CRC; partial functional loss).
FT                                {ECO:0000269|PubMed:10537275}.
FT                                /FTId=VAR_012959.
FT   VARIANT     580    580       S -> L (in dbSNP:rs41295270).
FT                                {ECO:0000269|PubMed:18033691}.
FT                                /FTId=VAR_038038.
FT   VARIANT     585    585       L -> P (mismatch repair deficient).
FT                                {ECO:0000269|PubMed:22581703}.
FT                                /FTId=VAR_068711.
FT   VARIANT     610    610       K -> N (associated with HNPCC5; unknown
FT                                pathological significance; repair
FT                                proficient).
FT                                {ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_067296.
FT   VARIANT     619    619       E -> D (in CRC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:15483016}.
FT                                /FTId=VAR_043952.
FT   VARIANT     623    623       P -> A (in dbSNP:rs3136334).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_029244.
FT   VARIANT     623    623       P -> L (no impairment of
FT                                heterodimerization with MSH2 and of in
FT                                vitro mismatch repair capacity).
FT                                {ECO:0000269|PubMed:15354210}.
FT                                /FTId=VAR_043953.
FT   VARIANT     677    677       S -> T (mismatch repair proficient).
FT                                {ECO:0000269|PubMed:22581703}.
FT                                /FTId=VAR_068712.
FT   VARIANT     685    685       G -> A (in CRC).
FT                                {ECO:0000269|PubMed:11470537}.
FT                                /FTId=VAR_043954.
FT   VARIANT     698    698       Q -> E (in HNPCC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:10480359}.
FT                                /FTId=VAR_012960.
FT   VARIANT     725    725       I -> M (in CRC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:11709755}.
FT                                /FTId=VAR_043955.
FT   VARIANT     728    728       K -> T (no impairment of
FT                                heterodimerization with MSH2 and of in
FT                                vitro mismatch repair capacity;
FT                                dbSNP:rs35552856).
FT                                {ECO:0000269|PubMed:15354210}.
FT                                /FTId=VAR_043956.
FT   VARIANT     772    772       R -> Q (in CRC).
FT                                {ECO:0000269|PubMed:11470537}.
FT                                /FTId=VAR_043957.
FT   VARIANT     772    772       R -> W (in HNPCC5).
FT                                {ECO:0000269|PubMed:14974087}.
FT                                /FTId=VAR_043958.
FT   VARIANT     787    787       A -> V (in CRC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:15483016}.
FT                                /FTId=VAR_043959.
FT   VARIANT     800    800       V -> A (in CRC; somatic mutation).
FT                                {ECO:0000269|PubMed:11470537}.
FT                                /FTId=VAR_043960.
FT   VARIANT     800    800       V -> L (may be a rare polymorphism).
FT                                {ECO:0000269|PubMed:10537275}.
FT                                /FTId=VAR_012961.
FT   VARIANT     803    803       D -> G (in CRC).
FT                                {ECO:0000269|PubMed:10537275}.
FT                                /FTId=VAR_012962.
FT   VARIANT     850    850       Y -> C (associated with HNPCC5 and CRC;
FT                                unknown pathological significance; repair
FT                                proficient).
FT                                {ECO:0000269|PubMed:10521294,
FT                                ECO:0000269|PubMed:11709755,
FT                                ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_012963.
FT   VARIANT     854    854       K -> M (in CRC; unknown pathological
FT                                significance; dbSNP:rs34374438).
FT                                {ECO:0000269|PubMed:11470537,
FT                                ECO:0000269|PubMed:14520694}.
FT                                /FTId=VAR_043961.
FT   VARIANT     878    878       V -> A (in suspected HNPCC5, colorectal/
FT                                endometrial cancer and CRC; repair
FT                                proficient; dbSNP:rs2020912).
FT                                {ECO:0000269|PubMed:11153917,
FT                                ECO:0000269|PubMed:11470537,
FT                                ECO:0000269|PubMed:11586295,
FT                                ECO:0000269|PubMed:11709755,
FT                                ECO:0000269|PubMed:14520694,
FT                                ECO:0000269|PubMed:15483016,
FT                                ECO:0000269|PubMed:18033691,
FT                                ECO:0000269|PubMed:22102614,
FT                                ECO:0000269|PubMed:22581703}.
FT                                /FTId=VAR_012964.
FT   VARIANT     886    886       I -> V (in dbSNP:rs2020914).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_014902.
FT   VARIANT     901    901       R -> H (in colorectal/endometrial
FT                                cancer). {ECO:0000269|PubMed:11153917}.
FT                                /FTId=VAR_043962.
FT   VARIANT     976    976       R -> H (in CRC; sporadic; also associated
FT                                with HNPCC5; repair proficient).
FT                                {ECO:0000269|PubMed:11807791,
FT                                ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_012965.
FT   VARIANT    1021   1021       A -> D (in CRC; unknown pathological
FT                                significance; repair proficient).
FT                                {ECO:0000269|PubMed:11709755,
FT                                ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_043963.
FT   VARIANT    1026   1026       D -> Y (associated with HNPCC5; unknown
FT                                pathological significance; repair
FT                                proficient).
FT                                {ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_067297.
FT   VARIANT    1031   1031       D -> V (in CRC; somatic mutation).
FT                                {ECO:0000269|PubMed:11470537}.
FT                                /FTId=VAR_043964.
FT   VARIANT    1076   1076       R -> C (in CRC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:15483016}.
FT                                /FTId=VAR_043965.
FT   VARIANT    1087   1087       P -> S (associated with HNPCC5; unknown
FT                                pathological significance; repair
FT                                proficient; dbSNP:rs63750998).
FT                                {ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_067298.
FT   VARIANT    1087   1087       P -> T (in CRC; dbSNP:rs63750998).
FT                                {ECO:0000269|PubMed:10537275}.
FT                                /FTId=VAR_012966.
FT   VARIANT    1095   1095       R -> H (in CRC; unknown pathological
FT                                significance; mismatch repair
FT                                proficient).
FT                                {ECO:0000269|PubMed:12522549,
FT                                ECO:0000269|PubMed:22581703}.
FT                                /FTId=VAR_043966.
FT   VARIANT    1100   1100       T -> M (in CRC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:11709755}.
FT                                /FTId=VAR_043967.
FT   VARIANT    1158   1158       C -> R (in CRC; somatic mutation).
FT                                {ECO:0000269|PubMed:11470537}.
FT                                /FTId=VAR_043968.
FT   VARIANT    1163   1163       E -> V (in HNPCC5; dbSNP:rs63750252).
FT                                {ECO:0000269|PubMed:15365995}.
FT                                /FTId=VAR_043969.
FT   VARIANT    1193   1193       E -> K (found in an endometrial cancer
FT                                sample; displays marked impairment of
FT                                heterodimerization with MSH2 and of in
FT                                vitro mismatch repair capacity).
FT                                {ECO:0000269|PubMed:15354210}.
FT                                /FTId=VAR_043970.
FT   VARIANT    1213   1213       D -> V. {ECO:0000269|PubMed:7604266}.
FT                                /FTId=VAR_004491.
FT   VARIANT    1219   1219       T -> I (in CRC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:11709755}.
FT                                /FTId=VAR_043971.
FT   VARIANT    1225   1225       T -> M (associated with HNPCC5; unknown
FT                                pathological significance; repair
FT                                proficient).
FT                                {ECO:0000269|PubMed:22102614}.
FT                                /FTId=VAR_067299.
FT   VARIANT    1232   1232       V -> L (in dbSNP:rs41295276).
FT                                {ECO:0000269|PubMed:18033691}.
FT                                /FTId=VAR_038039.
FT   VARIANT    1234   1234       E -> Q (in dbSNP:rs35717727).
FT                                /FTId=VAR_038040.
FT   VARIANT    1248   1248       H -> D (in CRC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:11709755}.
FT                                /FTId=VAR_043972.
FT   VARIANT    1260   1260       V -> I. {ECO:0000269|PubMed:7604266}.
FT                                /FTId=VAR_004492.
FT   VARIANT    1284   1284       T -> M (in CRC).
FT                                {ECO:0000269|PubMed:10413423}.
FT                                /FTId=VAR_043973.
FT   VARIANT    1321   1321       R -> G (in dbSNP:rs41295278).
FT                                {ECO:0000269|PubMed:18033691}.
FT                                /FTId=VAR_038041.
FT   VARIANT    1354   1354       L -> Q (in CRC; unknown pathological
FT                                significance; mismatch repair
FT                                proficient).
FT                                {ECO:0000269|PubMed:12522549,
FT                                ECO:0000269|PubMed:22581703}.
FT                                /FTId=VAR_043974.
FT   MUTAGEN     103    103       Y->A: Abolishes binding to H3K36me3 and
FT                                DNA mismatch repair activity.
FT                                {ECO:0000269|PubMed:23622243}.
FT   MUTAGEN     105    106       WW->AA: Abolishes binding to H3K36me3 and
FT                                DNA mismatch repair activity.
FT                                {ECO:0000269|PubMed:23622243}.
FT   MUTAGEN    1140   1140       K->R: No effect on mismatch binding,
FT                                complete loss of DNA repair function when
FT                                associated with MSH2 mutant R-675.
FT                                {ECO:0000269|PubMed:9564049}.
FT   CONFLICT     36     57       AAPGASPSPGGDAAWSEAGPGP -> GCPRGLSFPRRGCGL
FT                                ERGWAWA (in Ref. 2; BAA23674/BAA23675).
FT                                {ECO:0000305}.
FT   CONFLICT    868    868       M -> V (in Ref. 3; BAG65496).
FT                                {ECO:0000305}.
FT   CONFLICT   1358   1360       KEL -> D (in Ref. 4; AAL87401).
FT                                {ECO:0000305}.
FT   STRAND       74     79       {ECO:0000244|PDB:2GFU}.
FT   STRAND       94     98       {ECO:0000244|PDB:2GFU}.
FT   STRAND      106    109       {ECO:0000244|PDB:2GFU}.
FT   STRAND      120    125       {ECO:0000244|PDB:2GFU}.
FT   STRAND      127    133       {ECO:0000244|PDB:2GFU}.
FT   STRAND      135    137       {ECO:0000244|PDB:2GFU}.
FT   STRAND      139    143       {ECO:0000244|PDB:2GFU}.
FT   HELIX       145    147       {ECO:0000244|PDB:2GFU}.
FT   STRAND      148    151       {ECO:0000244|PDB:2GFU}.
FT   TURN        157    159       {ECO:0000244|PDB:2GFU}.
FT   HELIX       170    183       {ECO:0000244|PDB:2GFU}.
FT   HELIX       187    191       {ECO:0000244|PDB:2GFU}.
FT   TURN        192    195       {ECO:0000244|PDB:2GFU}.
FT   STRAND      197    199       {ECO:0000244|PDB:2GFU}.
FT   HELIX       366    369       {ECO:0000244|PDB:2O8B}.
FT   HELIX       371    373       {ECO:0000244|PDB:2O8B}.
FT   TURN        375    377       {ECO:0000244|PDB:2O8B}.
FT   HELIX       400    403       {ECO:0000244|PDB:2O8B}.
FT   HELIX       408    419       {ECO:0000244|PDB:2O8B}.
FT   STRAND      423    429       {ECO:0000244|PDB:2O8B}.
FT   STRAND      432    436       {ECO:0000244|PDB:2O8B}.
FT   HELIX       437    447       {ECO:0000244|PDB:2O8B}.
FT   STRAND      453    456       {ECO:0000244|PDB:2O8B}.
FT   STRAND      458    462       {ECO:0000244|PDB:2O8B}.
FT   HELIX       463    465       {ECO:0000244|PDB:2O8B}.
FT   HELIX       466    475       {ECO:0000244|PDB:2O8B}.
FT   STRAND      480    485       {ECO:0000244|PDB:2O8B}.
FT   HELIX       489    497       {ECO:0000244|PDB:2O8B}.
FT   HELIX       505    507       {ECO:0000244|PDB:2O8B}.
FT   STRAND      511    517       {ECO:0000244|PDB:2O8B}.
FT   HELIX       519    521       {ECO:0000244|PDB:2O8F}.
FT   STRAND      526    528       {ECO:0000244|PDB:2O8D}.
FT   STRAND      538    546       {ECO:0000244|PDB:2O8B}.
FT   STRAND      554    561       {ECO:0000244|PDB:2O8B}.
FT   TURN        563    565       {ECO:0000244|PDB:2O8B}.
FT   STRAND      568    575       {ECO:0000244|PDB:2O8B}.
FT   HELIX       580    588       {ECO:0000244|PDB:2O8B}.
FT   STRAND      591    597       {ECO:0000244|PDB:2O8B}.
FT   TURN        598    600       {ECO:0000244|PDB:2O8B}.
FT   HELIX       603    609       {ECO:0000244|PDB:2O8B}.
FT   TURN        610    615       {ECO:0000244|PDB:2O8B}.
FT   STRAND      616    621       {ECO:0000244|PDB:2O8B}.
FT   TURN        624    626       {ECO:0000244|PDB:2O8B}.
FT   HELIX       630    639       {ECO:0000244|PDB:2O8B}.
FT   TURN        640    643       {ECO:0000244|PDB:2O8B}.
FT   STRAND      644    647       {ECO:0000244|PDB:2O8B}.
FT   HELIX       657    661       {ECO:0000244|PDB:2O8B}.
FT   STRAND      667    669       {ECO:0000244|PDB:2O8F}.
FT   STRAND      671    673       {ECO:0000244|PDB:2O8B}.
FT   HELIX       675    677       {ECO:0000244|PDB:2O8B}.
FT   HELIX       678    693       {ECO:0000244|PDB:2O8B}.
FT   HELIX       697    701       {ECO:0000244|PDB:2O8B}.
FT   STRAND      706    708       {ECO:0000244|PDB:2O8B}.
FT   HELIX       712    715       {ECO:0000244|PDB:2O8B}.
FT   HELIX       737    742       {ECO:0000244|PDB:2O8B}.
FT   STRAND      746    748       {ECO:0000244|PDB:2O8F}.
FT   STRAND      750    753       {ECO:0000244|PDB:2O8B}.
FT   HELIX       758    762       {ECO:0000244|PDB:2O8B}.
FT   HELIX       768    779       {ECO:0000244|PDB:2O8B}.
FT   HELIX       785    799       {ECO:0000244|PDB:2O8B}.
FT   HELIX       802    812       {ECO:0000244|PDB:2O8B}.
FT   HELIX       818    829       {ECO:0000244|PDB:2O8B}.
FT   HELIX       831    836       {ECO:0000244|PDB:2O8B}.
FT   HELIX       838    841       {ECO:0000244|PDB:2O8B}.
FT   HELIX       847    879       {ECO:0000244|PDB:2O8B}.
FT   HELIX       885    890       {ECO:0000244|PDB:2O8B}.
FT   TURN        894    896       {ECO:0000244|PDB:2O8B}.
FT   STRAND      897    900       {ECO:0000244|PDB:2O8B}.
FT   HELIX       906    913       {ECO:0000244|PDB:2O8B}.
FT   HELIX       918    923       {ECO:0000244|PDB:2O8B}.
FT   HELIX       936    955       {ECO:0000244|PDB:2O8B}.
FT   HELIX       959    961       {ECO:0000244|PDB:2O8B}.
FT   STRAND      968    970       {ECO:0000244|PDB:2O8B}.
FT   HELIX       973    975       {ECO:0000244|PDB:2O8B}.
FT   STRAND      978    981       {ECO:0000244|PDB:2O8B}.
FT   TURN        983    986       {ECO:0000244|PDB:2O8B}.
FT   STRAND      995    999       {ECO:0000244|PDB:2O8B}.
FT   STRAND     1002   1005       {ECO:0000244|PDB:2O8B}.
FT   TURN       1008   1010       {ECO:0000244|PDB:2O8B}.
FT   HELIX      1011   1041       {ECO:0000244|PDB:2O8B}.
FT   HELIX      1044   1066       {ECO:0000244|PDB:2O8B}.
FT   STRAND     1070   1072       {ECO:0000244|PDB:2O8B}.
FT   TURN       1082   1084       {ECO:0000244|PDB:2O8B}.
FT   STRAND     1089   1094       {ECO:0000244|PDB:2O8B}.
FT   STRAND     1111   1116       {ECO:0000244|PDB:2O8B}.
FT   STRAND     1120   1122       {ECO:0000244|PDB:2O8F}.
FT   STRAND     1129   1133       {ECO:0000244|PDB:2O8B}.
FT   STRAND     1136   1138       {ECO:0000244|PDB:2O8F}.
FT   HELIX      1140   1154       {ECO:0000244|PDB:2O8B}.
FT   TURN       1155   1157       {ECO:0000244|PDB:2O8B}.
FT   STRAND     1160   1167       {ECO:0000244|PDB:2O8B}.
FT   STRAND     1171   1176       {ECO:0000244|PDB:2O8B}.
FT   HELIX      1189   1203       {ECO:0000244|PDB:2O8B}.
FT   STRAND     1209   1213       {ECO:0000244|PDB:2O8B}.
FT   TURN       1215   1218       {ECO:0000244|PDB:2O8B}.
FT   HELIX      1221   1237       {ECO:0000244|PDB:2O8B}.
FT   STRAND     1242   1246       {ECO:0000244|PDB:2O8B}.
FT   HELIX      1250   1255       {ECO:0000244|PDB:2O8B}.
FT   TURN       1256   1258       {ECO:0000244|PDB:2O8F}.
FT   STRAND     1260   1269       {ECO:0000244|PDB:2O8B}.
FT   STRAND     1285   1292       {ECO:0000244|PDB:2O8B}.
FT   HELIX      1298   1305       {ECO:0000244|PDB:2O8B}.
FT   HELIX      1310   1322       {ECO:0000244|PDB:2O8B}.
FT   TURN       1323   1326       {ECO:0000244|PDB:2O8F}.
FT   TURN       1330   1332       {ECO:0000244|PDB:2O8B}.
SQ   SEQUENCE   1360 AA;  152786 MW;  4A4AA9F8ECB8FFE9 CRC64;
     MSRQSTLYSF FPKSPALSDA NKASARASRE GGRAAAAPGA SPSPGGDAAW SEAGPGPRPL
     ARSASPPKAK NLNGGLRRSV APAAPTSCDF SPGDLVWAKM EGYPWWPCLV YNHPFDGTFI
     REKGKSVRVH VQFFDDSPTR GWVSKRLLKP YTGSKSKEAQ KGGHFYSAKP EILRAMQRAD
     EALNKDKIKR LELAVCDEPS EPEEEEEMEV GTTYVTDKSE EDNEIESEEE VQPKTQGSRR
     SSRQIKKRRV ISDSESDIGG SDVEFKPDTK EEGSSDEISS GVGDSESEGL NSPVKVARKR
     KRMVTGNGSL KRKSSRKETP SATKQATSIS SETKNTLRAF SAPQNSESQA HVSGGGDDSS
     RPTVWYHETL EWLKEEKRRD EHRRRPDHPD FDASTLYVPE DFLNSCTPGM RKWWQIKSQN
     FDLVICYKVG KFYELYHMDA LIGVSELGLV FMKGNWAHSG FPEIAFGRYS DSLVQKGYKV
     ARVEQTETPE MMEARCRKMA HISKYDRVVR REICRIITKG TQTYSVLEGD PSENYSKYLL
     SLKEKEEDSS GHTRAYGVCF VDTSLGKFFI GQFSDDRHCS RFRTLVAHYP PVQVLFEKGN
     LSKETKTILK SSLSCSLQEG LIPGSQFWDA SKTLRTLLEE EYFREKLSDG IGVMLPQVLK
     GMTSESDSIG LTPGEKSELA LSALGGCVFY LKKCLIDQEL LSMANFEEYI PLDSDTVSTT
     RSGAIFTKAY QRMVLDAVTL NNLEIFLNGT NGSTEGTLLE RVDTCHTPFG KRLLKQWLCA
     PLCNHYAIND RLDAIEDLMV VPDKISEVVE LLKKLPDLER LLSKIHNVGS PLKSQNHPDS
     RAIMYEETTY SKKKIIDFLS ALEGFKVMCK IIGIMEEVAD GFKSKILKQV ISLQTKNPEG
     RFPDLTVELN RWDTAFDHEK ARKTGLITPK AGFDSDYDQA LADIRENEQS LLEYLEKQRN
     RIGCRTIVYW GIGRNRYQLE IPENFTTRNL PEEYELKSTK KGCKRYWTKT IEKKLANLIN
     AEERRDVSLK DCMRRLFYNF DKNYKDWQSA VECIAVLDVL LCLANYSRGG DGPMCRPVIL
     LPEDTPPFLE LKGSRHPCIT KTFFGDDFIP NDILIGCEEE EQENGKAYCV LVTGPNMGGK
     STLMRQAGLL AVMAQMGCYV PAEVCRLTPI DRVFTRLGAS DRIMSGESTF FVELSETASI
     LMHATAHSLV LVDELGRGTA TFDGTAIANA VVKELAETIK CRTLFSTHYH SLVEDYSQNV
     AVRLGHMACM VENECEDPSQ ETITFLYKFI KGACPKSYGF NAARLANLPE EVIQKGHRKA
     REFEKMNQSL RLFREVCLAS ERSTVDAEAV HKLLTLIKEL
//
ID   MSH6_YEAST              Reviewed;        1242 AA.
AC   Q03834; D6VS82;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   11-NOV-2015, entry version 142.
DE   RecName: Full=DNA mismatch repair protein MSH6;
DE   AltName: Full=MutS protein homolog 6;
DE   AltName: Full=Postmeiotic segregation protein 3;
GN   Name=MSH6; Synonyms=PMS3; OrderedLocusNames=YDR097C;
GN   ORFNames=YD8557.04C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=8723353; DOI=10.1016/S0960-9822(02)00516-X;
RA   Iaccarino I., Palombo F., Drummond J.T., Totty N.F., Hsuan J.J.,
RA   Modrich P., Jiricny J.;
RT   "MSH6, a Saccharomyces cerevisiae protein that binds to mismatches as
RT   a heterodimer with MSH2.";
RL   Curr. Biol. 6:484-486(1996).
RN   [4]
RP   FUNCTION, INTERACTION WITH MSH2, AND MUTAGENESIS OF GLY-421.
RX   PubMed=8600025; DOI=10.1101/gad.10.4.407;
RA   Marsischky G.T., Filosi N., Kane M.F., Kolodner R.D.;
RT   "Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-
RT   dependent mismatch repair.";
RL   Genes Dev. 10:407-420(1996).
RN   [5]
RP   CHARACTERIZATION, AND INTERACTION WITH MSH2.
RX   PubMed=8816473;
RA   Alani E.;
RT   "The Saccharomyces cerevisiae Msh2 and Msh6 proteins form a complex
RT   that specifically binds to duplex oligonucleotides containing
RT   mismatched DNA base pairs.";
RL   Mol. Cell. Biol. 16:5604-5615(1996).
RN   [6]
RP   FUNCTION IN MMR.
RX   PubMed=9111357;
RA   Sia E.A., Kokoska R.J., Dominska M., Greenwell P., Petes T.D.;
RT   "Microsatellite instability in yeast: dependence on repeat unit size
RT   and DNA mismatch repair genes.";
RL   Mol. Cell. Biol. 17:2851-2858(1997).
RN   [7]
RP   FUNCTION, DNA-BINDING, AND COMPLEX FORMATION WITH MLH1-PMS1.
RX   PubMed=9545323; DOI=10.1074/jbc.273.16.9837;
RA   Habraken Y., Sung P., Prakash L., Prakash S.;
RT   "ATP-dependent assembly of a ternary complex consisting of a DNA
RT   mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes.";
RL   J. Biol. Chem. 273:9837-9841(1998).
RN   [8]
RP   MUTAGENESIS OF GLY-987.
RX   PubMed=9819445;
RA   Studamire B., Quach T., Alani E.;
RT   "Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both
RT   required during mismatch repair.";
RL   Mol. Cell. Biol. 18:7590-7601(1998).
RN   [9]
RP   FUNCTION.
RX   PubMed=9770499; DOI=10.1073/pnas.95.21.12404;
RA   Flores-Rozas H., Kolodner R.D.;
RT   "The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent
RT   suppression of frameshift mutations.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12404-12409(1998).
RN   [10]
RP   MUTAGENESIS OF LEU-301 AND GLY-477.
RX   PubMed=10537275;
RA   Kolodner R.D., Tytell J.D., Schmeits J.L., Kane M.F., Das Gupta R.,
RA   Weger J., Wahlberg S., Fox E.A., Peel D., Ziogas A., Garber J.E.,
RA   Syngal S., Anton-Culver H., Li F.P.;
RT   "Germ-line msh6 mutations in colorectal cancer families.";
RL   Cancer Res. 59:5068-5074(1999).
RN   [11]
RP   DNA-BINDING SPECIFICITY.
RX   PubMed=10066781; DOI=10.1074/jbc.274.11.7200;
RA   Marsischky G.T., Lee S., Griffith J., Kolodner R.D.;
RT   "Saccharomyces cerevisiae MSH2/6 complex interacts with Holliday
RT   junctions and facilitates their cleavage by phage resolution
RT   enzymes.";
RL   J. Biol. Chem. 274:7200-7206(1999).
RN   [12]
RP   MUTAGENESIS OF PHE-337.
RX   PubMed=10347163; DOI=10.1074/jbc.274.23.16115;
RA   Bowers J., Sokolsky T., Quach T., Alani E.;
RT   "A mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-
RT   MSH6 complex disrupts mismatch recognition.";
RL   J. Biol. Chem. 274:16115-16125(1999).
RN   [13]
RP   DNA-BINDING SPECIFICITY.
RX   PubMed=10480869; DOI=10.1074/jbc.274.38.26668;
RA   Marsischky G.T., Kolodner R.D.;
RT   "Biochemical characterization of the interaction between the
RT   Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in
RT   DNA.";
RL   J. Biol. Chem. 274:26668-26682(1999).
RN   [14]
RP   FUNCTION.
RX   PubMed=10518225; DOI=10.1016/S1097-2765(00)80346-9;
RA   Ni T.T., Marsischky G.T., Kolodner R.D.;
RT   "MSH2 and MSH6 are required for removal of adenine misincorporated
RT   opposite 8-oxo-guanine in S. cerevisiae.";
RL   Mol. Cell 4:439-444(1999).
RN   [15]
RP   INTERACTION WITH POL30, AND MUTAGENESIS OF 26-LYS-GLN-27 AND
RP   33-PHE-PHE-34.
RX   PubMed=11005803; DOI=10.1074/jbc.C000513200;
RA   Clark A.B., Valle F., Drotschmann K., Gary R.K., Kunkel T.A.;
RT   "Functional interaction of proliferating cell nuclear antigen with
RT   MSH2-MSH6 and MSH2-MSH3 complexes.";
RL   J. Biol. Chem. 275:36498-36501(2000).
RN   [16]
RP   FUNCTION, AND MUTAGENESIS OF PHE-337.
RX   PubMed=10970737; DOI=10.1006/jmbi.2000.4081;
RA   Bowers J., Tran P.T., Liskay R.M., Alani E.;
RT   "Analysis of yeast MSH2-MSH6 suggests that the initiation of mismatch
RT   repair can be separated into discrete steps.";
RL   J. Mol. Biol. 302:327-338(2000).
RN   [17]
RP   MUTAGENESIS.
RX   PubMed=10615127; DOI=10.1038/71684;
RA   Das Gupta R., Kolodner R.D.;
RT   "Novel dominant mutations in Saccharomyces cerevisiae MSH6.";
RL   Nat. Genet. 24:53-56(2000).
RN   [18]
RP   INTERACTION WITH POL30, AND MUTAGENESIS OF 33-PHE-PHE-34.
RX   PubMed=11062484; DOI=10.1038/81708;
RA   Flores-Rozas H., Clark D., Kolodner R.D.;
RT   "Proliferating cell nuclear antigen and Msh2p-Msh6p interact to form
RT   an active mispair recognition complex.";
RL   Nat. Genet. 26:375-378(2000).
RN   [19]
RP   DNA-BINDING, AND MUTAGENESIS OF PRO-313; PHE-337; GLU-339; GLY-368;
RP   PRO-370; GLN-393; ARG-412; LYS-848 AND ARG-852.
RX   PubMed=11641390; DOI=10.1074/jbc.C100450200;
RA   Drotschmann K., Yang W., Brownewell F.E., Kool E.T., Kunkel T.A.;
RT   "Asymmetric recognition of DNA local distortion. Structure-based
RT   functional studies of eukaryotic Msh2-Msh6.";
RL   J. Biol. Chem. 276:46225-46229(2001).
RN   [20]
RP   FUNCTION, AND COMPLEX FORMATION WITH MLH1-PMS1.
RX   PubMed=11237611; DOI=10.1006/jmbi.2001.4467;
RA   Bowers J., Tran P.T., Joshi A., Liskay R.M., Alani E.;
RT   "MSH-MLH complexes formed at a DNA mismatch are disrupted by the PCNA
RT   sliding clamp.";
RL   J. Mol. Biol. 306:957-968(2001).
RN   [21]
RP   FUNCTION, AND MUTAGENESIS OF GLU-1062.
RX   PubMed=12509278; DOI=10.1016/S1568-7864(02)00081-2;
RA   Drotschmann K., Yang W., Kunkel T.A.;
RT   "Evidence for sequential action of two ATPase active sites in yeast
RT   Msh2-Msh6.";
RL   DNA Repair 1:743-753(2002).
RN   [22]
RP   MUTAGENESIS OF SER-1036; GLY-1067; HIS-1096 AND GLY-1142.
RX   PubMed=11986324; DOI=10.1074/jbc.M202282200;
RA   Hess M.T., Das Gupta R., Kolodner R.D.;
RT   "Dominant Saccharomyces cerevisiae msh6 mutations cause increased
RT   mispair binding and decreased dissociation from mispairs by Msh2-Msh6
RT   in the presence of ATP.";
RL   J. Biol. Chem. 277:25545-25553(2002).
RN   [23]
RP   FUNCTION.
RX   PubMed=12820877; DOI=10.1021/bi034602h;
RA   Antony E., Hingorani M.M.;
RT   "Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-
RT   bound state at the initiation of DNA repair.";
RL   Biochemistry 42:7682-7693(2003).
RN   [24]
RP   INTERACTION WITH POL30.
RX   PubMed=12435741; DOI=10.1074/jbc.C200627200;
RA   Lau P.J., Kolodner R.D.;
RT   "Transfer of the MSH2.MSH6 complex from proliferating cell nuclear
RT   antigen to mispaired bases in DNA.";
RL   J. Biol. Chem. 278:14-17(2003).
RN   [25]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [26]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [27]
RP   ENZYME REGULATION, AND MUTAGENESIS OF GLU-1062.
RX   PubMed=15513922; DOI=10.1074/jbc.C400495200;
RA   Clark A.B., Kunkel T.A.;
RT   "Cadmium inhibits the functions of eukaryotic MutS complexes.";
RL   J. Biol. Chem. 279:53903-53906(2004).
RN   [28]
RP   FUNCTION, AND COMPLEX FORMATION WITH MLH1-PMS1.
RX   PubMed=15811858; DOI=10.1074/jbc.M407545200;
RA   Mendillo M.L., Mazur D.J., Kolodner R.D.;
RT   "Analysis of the interaction between the Saccharomyces cerevisiae
RT   MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-
RT   blocking system.";
RL   J. Biol. Chem. 280:22245-22257(2005).
RN   [29]
RP   FUNCTION.
RX   PubMed=16337600; DOI=10.1016/j.molcel.2005.10.014;
RA   Jiang J., Bai L., Surtees J.A., Gemici Z., Wang M.D., Alani E.;
RT   "Detection of high-affinity and sliding clamp modes for MSH2-MSH6 by
RT   single-molecule unzipping force analysis.";
RL   Mol. Cell 20:771-781(2005).
RN   [30]
RP   ENZYME REGULATION.
RX   PubMed=15746000; DOI=10.1093/nar/gki291;
RA   Banerjee S., Flores-Rozas H.;
RT   "Cadmium inhibits mismatch repair by blocking the ATPase activity of
RT   the MSH2-MSH6 complex.";
RL   Nucleic Acids Res. 33:1410-1419(2005).
RN   [31]
RP   FUNCTION, AND MUTAGENESIS OF LYS-988 AND GLU-1062.
RX   PubMed=16214425; DOI=10.1016/j.dnarep.2005.08.016;
RA   Antony E., Khubchandani S., Chen S., Hingorani M.M.;
RT   "Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and
RT   DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6
RT   mismatch repair protein.";
RL   DNA Repair 5:153-162(2006).
RN   [32]
RP   FUNCTION.
RX   PubMed=16702432; DOI=10.1534/genetics.106.055616;
RA   Stone J.E., Petes T.D.;
RT   "Analysis of the proteins involved in the in vivo repair of base-base
RT   mismatches and four-base loops formed during meiotic recombination in
RT   the yeast Saccharomyces cerevisiae.";
RL   Genetics 173:1223-1239(2006).
RN   [33]
RP   FUNCTION, AND MUTAGENESIS OF LYS-988.
RX   PubMed=16600868; DOI=10.1016/j.molcel.2006.02.010;
RA   Mazur D.J., Mendillo M.L., Kolodner R.D.;
RT   "Inhibition of Msh6 ATPase activity by mispaired DNA induces a
RT   Msh2(ATP)-Msh6(ATP) state capable of hydrolysis-independent movement
RT   along DNA.";
RL   Mol. Cell 22:39-49(2006).
RN   [34]
RP   FUNCTION, AND MUTAGENESIS OF SER-1036; GLY-1067 AND GLY-1142.
RX   PubMed=16407100; DOI=10.1073/pnas.0510078103;
RA   Hess M.T., Mendillo M.L., Mazur D.J., Kolodner R.D.;
RT   "Biochemical basis for dominant mutations in the Saccharomyces
RT   cerevisiae MSH6 gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:558-563(2006).
RN   [35]
RP   FUNCTION, AND MUTAGENESIS OF GLU-339.
RX   PubMed=17141577; DOI=10.1016/j.dnarep.2006.10.023;
RA   Holmes S.F., Scarpinato K.D., McCulloch S.D., Schaaper R.M.,
RA   Kunkel T.A.;
RT   "Specialized mismatch repair function of Glu339 in the Phe-X-Glu motif
RT   of yeast Msh6.";
RL   DNA Repair 6:293-303(2007).
RN   [36]
RP   FUNCTION.
RX   PubMed=17157869; DOI=10.1016/j.jmb.2006.10.099;
RA   Lee S.D., Surtees J.A., Alani E.;
RT   "Saccharomyces cerevisiae MSH2-MSH3 and MSH2-MSH6 complexes display
RT   distinct requirements for DNA binding domain I in mismatch
RT   recognition.";
RL   J. Mol. Biol. 366:53-66(2007).
RN   [37]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-150, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [38]
RP   FUNCTION, AND DNA-BINDING DOMAIN.
RX   PubMed=17567610; DOI=10.1093/nar/gkm409;
RA   Clark A.B., Deterding L., Tomer K.B., Kunkel T.A.;
RT   "Multiple functions for the N-terminal region of Msh6.";
RL   Nucleic Acids Res. 35:4114-4123(2007).
RN   [39]
RP   FUNCTION.
RX   PubMed=17573527; DOI=10.1073/pnas.0704148104;
RA   Shell S.S., Putnam C.D., Kolodner R.D.;
RT   "Chimeric Saccharomyces cerevisiae Msh6 protein with an Msh3 mispair-
RT   binding domain combines properties of both proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10956-10961(2007).
RN   [40]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [41]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-145; SER-150
RP   AND THR-451, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [42]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-150 AND
RP   SER-201, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Component of the post-replicative DNA mismatch repair
CC       system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which
CC       binds to DNA mismatches thereby initiating DNA repair. MSH6
CC       provides substrate-binding and substrate specificity to the
CC       complex. When bound, MutS alpha bends the DNA helix and shields
CC       approximately 20 base pairs. Acts mainly to repair base-base and
CC       single insertion-deletion mismatches that occur during
CC       replication, but can also repair longer insertion-deletion loops
CC       (IDLs), although with decreasing efficiency as the size of the
CC       extrahelical loop increases. After mismatch binding, forms a
CC       ternary complex with the MutL alpha heterodimer, which is thought
CC       to be responsible for directing the downstream MMR events,
CC       including strand discrimination, excision, and resynthesis. ATP
CC       binding and hydrolysis by the MutS alpha complex is crucial for
CC       MMR. Both subunits bind ATP, but with differing affinities, and
CC       their ATPase kinetics are also very different. MSH6 binds and
CC       hydrolyzes ATP rapidly, whereas MSH2 catalyzes ATP at a
CC       substantially slower rate. Binding to a mismatched base pair
CC       suppresses MSH6-catalyzed ATP hydrolysis, but not the activity of
CC       MSH2. ATP binding to both subunits is necessary to trigger a
CC       change in MutS alpha interaction with mismatched DNA, converting
CC       MutS alpha into a sliding clamp capable of hydrolysis-independent
CC       movement along DNA, and also facilitates formation of ternary
CC       complexes containing MutS and MutL proteins and the mismatch. May
CC       also be involved in resolution of recombination intermediates.
CC       {ECO:0000269|PubMed:10518225, ECO:0000269|PubMed:10970737,
CC       ECO:0000269|PubMed:11237611, ECO:0000269|PubMed:12509278,
CC       ECO:0000269|PubMed:12820877, ECO:0000269|PubMed:15811858,
CC       ECO:0000269|PubMed:16214425, ECO:0000269|PubMed:16337600,
CC       ECO:0000269|PubMed:16407100, ECO:0000269|PubMed:16600868,
CC       ECO:0000269|PubMed:16702432, ECO:0000269|PubMed:17141577,
CC       ECO:0000269|PubMed:17157869, ECO:0000269|PubMed:17567610,
CC       ECO:0000269|PubMed:17573527, ECO:0000269|PubMed:8600025,
CC       ECO:0000269|PubMed:9111357, ECO:0000269|PubMed:9545323,
CC       ECO:0000269|PubMed:9770499}.
CC   -!- ENZYME REGULATION: Inhibited by Cd(2+).
CC       {ECO:0000269|PubMed:15513922, ECO:0000269|PubMed:15746000}.
CC   -!- SUBUNIT: Heterodimer consisting of MSH2-MSH6 (MutS alpha). Forms a
CC       ternary complex with MutL alpha (MLH1-PMS1). MutS alpha interacts
CC       with proliferating cell nuclear antigen (PCNA/POL30). This
CC       interaction is disrupted upon binding of MutS alpha to mismatch
CC       DNA. {ECO:0000269|PubMed:11005803, ECO:0000269|PubMed:11062484,
CC       ECO:0000269|PubMed:12435741, ECO:0000269|PubMed:8600025,
CC       ECO:0000269|PubMed:8816473}.
CC   -!- INTERACTION:
CC       P25847:MSH2; NbExp=6; IntAct=EBI-11383, EBI-11352;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: The PIP box serves as a PCNA(POL30)-recognition and
CC       -binding motif.
CC   -!- MISCELLANEOUS: Present with 5330 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC       {ECO:0000305}.
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DR   EMBL; Z47746; CAA87671.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11942.1; -; Genomic_DNA.
DR   PIR; S51246; S51246.
DR   RefSeq; NP_010382.3; NM_001180405.3.
DR   ProteinModelPortal; Q03834; -.
DR   BioGrid; 32152; 60.
DR   DIP; DIP-2423N; -.
DR   IntAct; Q03834; 32.
DR   MINT; MINT-618151; -.
DR   MaxQB; Q03834; -.
DR   PeptideAtlas; Q03834; -.
DR   EnsemblFungi; YDR097C; YDR097C; YDR097C.
DR   GeneID; 851671; -.
DR   KEGG; sce:YDR097C; -.
DR   EuPathDB; FungiDB:YDR097C; -.
DR   SGD; S000002504; MSH6.
DR   GeneTree; ENSGT00550000075024; -.
DR   HOGENOM; HOG000189303; -.
DR   InParanoid; Q03834; -.
DR   KO; K08737; -.
DR   OMA; ALKDCMR; -.
DR   OrthoDB; EOG773XQH; -.
DR   BioCyc; YEAST:G3O-29700-MONOMER; -.
DR   Reactome; R-SCE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   NextBio; 969292; -.
DR   PRO; PR:Q03834; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   GO; GO:0032301; C:MutSalpha complex; IPI:SGD.
DR   GO; GO:0005524; F:ATP binding; IDA:SGD.
DR   GO; GO:0016887; F:ATPase activity; IDA:SGD.
DR   GO; GO:0000400; F:four-way junction DNA binding; IDA:SGD.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0036297; P:interstrand cross-link repair; IGI:SGD.
DR   GO; GO:0000710; P:meiotic mismatch repair; IMP:SGD.
DR   GO; GO:0006298; P:mismatch repair; IDA:SGD.
DR   Gene3D; 3.30.420.110; -; 1.
DR   Gene3D; 3.40.1170.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR   InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01624; MutS_I; 1.
DR   Pfam; PF05188; MutS_II; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF05190; MutS_IV; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53150; SSF53150; 1.
DR   SUPFAM; SSF55271; SSF55271; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN         1   1242       DNA mismatch repair protein MSH6.
FT                                /FTId=PRO_0000115213.
FT   DNA_BIND    228    299
FT   NP_BIND     982    989       ATP. {ECO:0000255}.
FT   REGION      305    421       Mispair-binding domain.
FT   MOTIF        27     34       PIP box.
FT   MOD_RES     102    102       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   MOD_RES     145    145       Phosphoserine.
FT                                {ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES     150    150       Phosphoserine.
FT                                {ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES     201    201       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     451    451       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   MUTAGEN      26     27       KQ->AA: Partially functional in a
FT                                mismatch repair assay; when associated
FT                                with 33-AA-34.
FT                                {ECO:0000269|PubMed:11005803}.
FT   MUTAGEN      33     34       FF->AA: Abolishes interaction with PCNA
FT                                (POL30), but only causes a moderate
FT                                mismatch repair defect. Partially
FT                                functional in a mismatch repair assay;
FT                                when associated with 26-AA-27.
FT                                {ECO:0000269|PubMed:11005803,
FT                                ECO:0000269|PubMed:11062484}.
FT   MUTAGEN     301    301       L->V: Fully functional in a mismatch
FT                                repair assay.
FT                                {ECO:0000269|PubMed:10537275}.
FT   MUTAGEN     313    313       P->A: Fully functional in a mismatch
FT                                repair assay.
FT                                {ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     337    337       F->A: Shows defects in both homoduplex
FT                                and mispair DNA binding and is only
FT                                partially functional in a mismatch repair
FT                                assay. {ECO:0000269|PubMed:10347163,
FT                                ECO:0000269|PubMed:10970737,
FT                                ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     337    337       F->H,I,Y: Partially functional in a
FT                                mismatch repair assay.
FT                                {ECO:0000269|PubMed:10347163,
FT                                ECO:0000269|PubMed:10970737,
FT                                ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     337    337       F->K: Completely abolishes mismatch
FT                                repair. {ECO:0000269|PubMed:10347163,
FT                                ECO:0000269|PubMed:10970737,
FT                                ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     337    337       F->S: In MSH6-6; partially functional in
FT                                a mismatch repair assay.
FT                                {ECO:0000269|PubMed:10347163,
FT                                ECO:0000269|PubMed:10970737,
FT                                ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     339    339       E->A: Defective in repairing 8-oxo-G-A
FT                                mismatches. {ECO:0000269|PubMed:11641390,
FT                                ECO:0000269|PubMed:17141577}.
FT   MUTAGEN     340    343       LYEK->CFAE: In MSH6-340; shows defects in
FT                                mispair DNA binding, but not in
FT                                homoduplex DNA binding.
FT                                {ECO:0000269|PubMed:10615127}.
FT   MUTAGEN     368    368       G->A: Moderately reduced activity in a
FT                                mismatch repair assay.
FT                                {ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     370    370       P->A: Partially functional in a mismatch
FT                                repair assay.
FT                                {ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     393    393       Q->A: Moderately reduced activity in a
FT                                mismatch repair assay.
FT                                {ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     393    393       Q->R: In MSH6-5; partially functional in
FT                                a mismatch repair assay.
FT                                {ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     412    412       R->A: Completely abolishes mismatch
FT                                repair. {ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     412    412       R->G: In MSH6-7; partially functional in
FT                                a mismatch repair assay.
FT                                {ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     421    421       G->D: In PMS3-1; completely abolishes
FT                                mismatch repair.
FT                                {ECO:0000269|PubMed:8600025}.
FT   MUTAGEN     477    477       G->R: Partially functional in a mismatch
FT                                repair assay.
FT                                {ECO:0000269|PubMed:10537275}.
FT   MUTAGEN     848    848       K->A: Fully functional in a mismatch
FT                                repair assay.
FT                                {ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     852    852       R->A: Moderately reduced activity in a
FT                                mismatch repair assay.
FT                                {ECO:0000269|PubMed:11641390}.
FT   MUTAGEN     987    987       G->D: Has no defect in mismatch DNA
FT                                binding, but lacks ATP-induced
FT                                conformational change.
FT                                {ECO:0000269|PubMed:9819445}.
FT   MUTAGEN     988    988       K->A: Impairs ATP binding; reduces
FT                                catalytic activity 13-fold for ATP
FT                                hydrolysis. {ECO:0000269|PubMed:16214425,
FT                                ECO:0000269|PubMed:16600868}.
FT   MUTAGEN    1036   1036       S->P: In MSH6-4; defective for ATP-
FT                                induced sliding clamp formation and
FT                                assembly of ternary complexes with MutL
FT                                alpha. {ECO:0000269|PubMed:11986324,
FT                                ECO:0000269|PubMed:16407100}.
FT   MUTAGEN    1062   1062       E->A: Reduces catalytic activity 13-fold
FT                                for ATP hydrolysis.
FT                                {ECO:0000269|PubMed:12509278,
FT                                ECO:0000269|PubMed:15513922,
FT                                ECO:0000269|PubMed:16214425}.
FT   MUTAGEN    1067   1067       G->D: In MSH6-3; defective for ATP-
FT                                induced sliding clamp formation and
FT                                assembly of ternary complexes with MutL
FT                                alpha. {ECO:0000269|PubMed:11986324,
FT                                ECO:0000269|PubMed:16407100}.
FT   MUTAGEN    1096   1096       H->A: In MSH6-9; shows normal mispair
FT                                binding and dissociation, but fails to
FT                                show complete mispair activation of the
FT                                ATPase. {ECO:0000269|PubMed:11986324}.
FT   MUTAGEN    1142   1142       G->D: In MSH6-2; defective for ATP-
FT                                induced sliding clamp formation, but
FT                                assembles ternary complexes with MutL
FT                                alpha. {ECO:0000269|PubMed:11986324,
FT                                ECO:0000269|PubMed:16407100}.
SQ   SEQUENCE   1242 AA;  140080 MW;  11A6883AADCFA222 CRC64;
     MAPATPKTSK TAHFENGSTS SQKKMKQSSL LSFFSKQVPS GTPSKKVQKP TPATLENTAT
     DKITKNPQGG KTGKLFVDVD EDNDLTIAEE TVSTVRSDIM HSQEPQSDTM LNSNTTEPKS
     TTTDEDLSSS QSRRNHKRRV NYAESDDDDS DTTFTAKRKK GKVVDSESDE DEYLPDKNDG
     DEDDDIADDK EDIKGELAED SGDDDDLISL AETTSKKKFS YNTSHSSSPF TRNISRDNSK
     KKSRPNQAPS RSYNPSHSQP SATSKSSKFN KQNEERYQWL VDERDAQRRP KSDPEYDPRT
     LYIPSSAWNK FTPFEKQYWE IKSKMWDCIV FFKKGKFFEL YEKDALLANA LFDLKIAGGG
     RANMQLAGIP EMSFEYWAAQ FIQMGYKVAK VDQRESMLAK EMREGSKGIV KRELQCILTS
     GTLTDGDMLH SDLATFCLAI REEPGNFYNE TQLDSSTIVQ KLNTKIFGAA FIDTATGELQ
     MLEFEDDSEC TKLDTLMSQV RPMEVVMERN NLSTLANKIV KFNSAPNAIF NEVKAGEEFY
     DCDKTYAEII SSEYFSTEED WPEVLKSYYD TGKKVGFSAF GGLLYYLKWL KLDKNLISMK
     NIKEYDFVKS QHSMVLDGIT LQNLEIFSNS FDGSDKGTLF KLFNRAITPM GKRMMKKWLM
     HPLLRKNDIE SRLDSVDSLL QDITLREQLE ITFSKLPDLE RMLARIHSRT IKVKDFEKVI
     TAFETIIELQ DSLKNNDLKG DVSKYISSFP EGLVEAVKSW TNAFERQKAI NENIIVPQRG
     FDIEFDKSMD RIQELEDELM EILMTYRKQF KCSNIQYKDS GKEIYTIEIP ISATKNVPSN
     WVQMAANKTY KRYYSDEVRA LARSMAEAKE IHKTLEEDLK NRLCQKFDAH YNTIWMPTIQ
     AISNIDCLLA ITRTSEYLGA PSCRPTIVDE VDSKTNTQLN GFLKFKSLRH PCFNLGATTA
     KDFIPNDIEL GKEQPRLGLL TGANAAGKST ILRMACIAVI MAQMGCYVPC ESAVLTPIDR
     IMTRLGANDN IMQGKSTFFV ELAETKKILD MATNRSLLVV DELGRGGSSS DGFAIAESVL
     HHVATHIQSL GFFATHYGTL ASSFKHHPQV RPLKMSILVD EATRNVTFLY KMLEGQSEGS
     FGMHVASMCG ISKEIIDNAQ IAADNLEHTS RLVKERDLAA NNLNGEVVSV PGGLQSDFVR
     IAYGDGLKNT KLGSGEGVLN YDWNIKRNVL KSLFSIIDDL QS
//
ID   RAD2_YEAST              Reviewed;        1031 AA.
AC   P07276; D6VV38; E9P8X9;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   11-NOV-2015, entry version 159.
DE   RecName: Full=DNA repair protein RAD2;
DE            EC=3.1.-.-;
GN   Name=RAD2; OrderedLocusNames=YGR258C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3000874; DOI=10.1016/0378-1119(85)90177-5;
RA   Nicolet C.M., Chenevert J.M., Friedberg E.C.;
RT   "The RAD2 gene of Saccharomyces cerevisiae: nucleotide sequence and
RT   transcript mapping.";
RL   Gene 36:225-234(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX   PubMed=3011752;
RA   Madura K., Prakash S.;
RT   "Nucleotide sequence, transcript mapping, and regulation of the RAD2
RT   gene of Saccharomyces cerevisiae.";
RL   J. Bacteriol. 166:914-923(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
RA   Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
RA   Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
RA   Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
RA   Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
RA   Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
RA   Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
RA   Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
RA   Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
RA   Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
RA   Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
RA   Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
RA   Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
RA   Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
RA   Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
RA   Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
RA   Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
RA   Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
RA   Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
RA   van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
RA   Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
RA   Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
RA   Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9090059;
RX   DOI=10.1002/(SICI)1097-0061(19970315)13:3<287::AID-YEA75>3.0.CO;2-5;
RA   Clemente M.L., Sartori G., Cardazzo B., Carignani G.;
RT   "Analysis of an 11.6 kb region from the right arm of chromosome VII of
RT   Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals
RT   the presence of three new genes.";
RL   Yeast 13:287-290(1997).
RN   [7]
RP   FUNCTION.
RX   PubMed=8247134; DOI=10.1038/366365a0;
RA   Habraken Y., Sung P., Prakash L., Prakash S.;
RT   "Yeast excision repair gene RAD2 encodes a single-stranded DNA
RT   endonuclease.";
RL   Nature 366:365-368(1993).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-367, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Single-stranded DNA endonuclease involved in excision
CC       repair of DNA damaged with UV light, bulky adducts, or cross-
CC       linking agents. Essential for the incision step of excision-
CC       repair. {ECO:0000269|PubMed:8247134}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. They probably participate
CC       in the reaction catalyzed by the enzyme. May bind an additional
CC       third magnesium ion after substrate binding. {ECO:0000250};
CC   -!- INTERACTION:
CC       Q00416:SEN1; NbExp=3; IntAct=EBI-14757, EBI-16945;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 846 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M10275; AAA66928.1; -; Genomic_DNA.
DR   EMBL; Y07777; CAA69080.1; -; Genomic_DNA.
DR   EMBL; Z73043; CAA97287.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08349.1; -; Genomic_DNA.
DR   EMBL; AY692857; AAT92876.1; -; Genomic_DNA.
DR   PIR; A29839; A29839.
DR   RefSeq; NP_011774.1; NM_001181387.1.
DR   PDB; 2LOX; NMR; -; B=642-690.
DR   PDB; 4Q0R; X-ray; 2.75 A; A/B=2-986.
DR   PDB; 4Q0W; X-ray; 2.10 A; A/B=2-986.
DR   PDB; 4Q0Z; X-ray; 2.40 A; A/B/E/F=2-986.
DR   PDB; 4Q10; X-ray; 2.70 A; A/B=2-986.
DR   PDBsum; 2LOX; -.
DR   PDBsum; 4Q0R; -.
DR   PDBsum; 4Q0W; -.
DR   PDBsum; 4Q0Z; -.
DR   PDBsum; 4Q10; -.
DR   ProteinModelPortal; P07276; -.
DR   SMR; P07276; 2-104, 762-983.
DR   BioGrid; 33510; 44.
DR   DIP; DIP-5869N; -.
DR   IntAct; P07276; 1.
DR   MINT; MINT-683829; -.
DR   MaxQB; P07276; -.
DR   PeptideAtlas; P07276; -.
DR   PRIDE; P07276; -.
DR   EnsemblFungi; YGR258C; YGR258C; YGR258C.
DR   GeneID; 853174; -.
DR   KEGG; sce:YGR258C; -.
DR   EuPathDB; FungiDB:YGR258C; -.
DR   SGD; S000003490; RAD2.
DR   GeneTree; ENSGT00640000091542; -.
DR   HOGENOM; HOG000214817; -.
DR   InParanoid; P07276; -.
DR   KO; K10846; -.
DR   OMA; FQATMRD; -.
DR   OrthoDB; EOG7QK0MK; -.
DR   BioCyc; YEAST:G3O-30928-MONOMER; -.
DR   Reactome; R-SCE-110302; Formation of transcription-coupled NER (TC-NER) repair complex.
DR   Reactome; R-SCE-110304; Dual incision reaction in TC-NER.
DR   Reactome; R-SCE-73935; Formation of incision complex in GG-NER.
DR   Reactome; R-SCE-73941; Dual incision reaction in GG-NER.
DR   NextBio; 973302; -.
DR   PRO; PR:P07276; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:SGD.
DR   GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; IDA:SGD.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IGI:SGD.
DR   Gene3D; 3.40.50.1010; -; 2.
DR   InterPro; IPR020045; 5-3_exonuclease_C.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN_domain-like.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   PRINTS; PR00066; XRODRMPGMNTG.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; SSF47807; 2.
DR   SUPFAM; SSF88723; SSF88723; 2.
DR   TIGRFAMs; TIGR00600; rad2; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; DNA damage; DNA repair; Endonuclease;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1   1031       DNA repair protein RAD2.
FT                                /FTId=PRO_0000154035.
FT   REGION        1     95       N-domain.
FT   REGION      756    884       I-domain.
FT   METAL        30     30       Magnesium 1. {ECO:0000250}.
FT   METAL        77     77       Magnesium 1. {ECO:0000250}.
FT   METAL       792    792       Magnesium 1. {ECO:0000250}.
FT   METAL       794    794       Magnesium 1. {ECO:0000250}.
FT   METAL       813    813       Magnesium 2. {ECO:0000250}.
FT   METAL       815    815       Magnesium 2. {ECO:0000250}.
FT   METAL       864    864       Magnesium 2. {ECO:0000250}.
FT   MOD_RES     118    118       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     367    367       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     583    583       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   CONFLICT    782    782       F -> L (in Ref. 5; AAT92876).
FT                                {ECO:0000305}.
FT   HELIX         6     10       {ECO:0000244|PDB:4Q0W}.
FT   HELIX        11     13       {ECO:0000244|PDB:4Q0W}.
FT   STRAND       15     18       {ECO:0000244|PDB:4Q0W}.
FT   HELIX        19     22       {ECO:0000244|PDB:4Q0W}.
FT   STRAND       26     30       {ECO:0000244|PDB:4Q0W}.
FT   HELIX        34     41       {ECO:0000244|PDB:4Q0W}.
FT   STRAND       45     49       {ECO:0000244|PDB:4Q0Z}.
FT   HELIX        53     67       {ECO:0000244|PDB:4Q0W}.
FT   STRAND       71     76       {ECO:0000244|PDB:4Q0W}.
FT   HELIX        82     96       {ECO:0000244|PDB:4Q0W}.
FT   STRAND      667    669       {ECO:0000244|PDB:2LOX}.
FT   HELIX       769    781       {ECO:0000244|PDB:4Q0W}.
FT   STRAND      786    788       {ECO:0000244|PDB:4Q0W}.
FT   HELIX       793    802       {ECO:0000244|PDB:4Q0W}.
FT   STRAND      807    810       {ECO:0000244|PDB:4Q0W}.
FT   HELIX       815    818       {ECO:0000244|PDB:4Q0W}.
FT   STRAND      823    827       {ECO:0000244|PDB:4Q0W}.
FT   STRAND      830    839       {ECO:0000244|PDB:4Q0W}.
FT   HELIX       840    847       {ECO:0000244|PDB:4Q0W}.
FT   HELIX       851    861       {ECO:0000244|PDB:4Q0W}.
FT   HELIX       874    884       {ECO:0000244|PDB:4Q0W}.
FT   HELIX       887    899       {ECO:0000244|PDB:4Q0W}.
FT   HELIX       901    904       {ECO:0000244|PDB:4Q0W}.
FT   HELIX       909    920       {ECO:0000244|PDB:4Q0W}.
FT   HELIX       932    939       {ECO:0000244|PDB:4Q0W}.
FT   HELIX       957    968       {ECO:0000244|PDB:4Q0W}.
FT   HELIX       972    982       {ECO:0000244|PDB:4Q0W}.
SQ   SEQUENCE   1031 AA;  117838 MW;  682D4AECFBD7F0F3 CRC64;
     MGVHSFWDIA GPTARPVRLE SLEDKRMAVD ASIWIYQFLK AVRDQEGNAV KNSHITGFFR
     RICKLLYFGI RPVFVFDGGV PVLKRETIRQ RKERRQGKRE SAKSTARKLL ALQLQNGSND
     NVKNSTPSSG SSVQIFKPQD EWDLPDIPGF KYDKEDARVN SNKTFEKLMN SINGDGLEDI
     DLDTINPASA EFEELPKATQ YLILSSLRLK SRLRMGYSKE QLETIFPNSM DFSRFQIDMV
     KRRNFFTQKL INTTGFQDGG ASKLNEEVIN RISGQKSKEY KLTKTNNGWI LGLGANDGSD
     AQKAIVIDDK DAGALVKQLD SNAEDGDVLR WDDLEDNSLK IVRHESSNAT TAPQKRSNRS
     EDEGCDSDEC EWEEVELKPK NVKFVEDFSL KAARLPYMGQ SLNNAGSKSF LDKRHDQASP
     SKTTPTMRIS RISVEDDDED YLKQIEEIEM MEAVQLSKME KKPEADDKSK IAKPVTSKGT
     EARPPIVQYG LLGAQPDSKQ PYHVTNLNSK SESVIKRTSK TVLSEFRPPS QQEDKGAILT
     EGEQNLNFIS HKIPQFDFNN ENSLLFQKNT ESNVSQEATK EKSPIPEMPS WFSSTASQQL
     YNPYNTTNFV EDKNVRNEQE SGAETTNKGS SYELLTGLNA TEILERESEK ESSNDENKDD
     DLEVLSEELF EDVPTKSQIS KEAEDNDSRK VESINKEHRK PLIFDYDFSE DEEDNIVENM
     IKEQEEFDTF KNTTLSTSAE RNVAENAFVE DELFEQQMKD KRDSDEVTMD MIKEVQELLS
     RFGIPYITAP MEAEAQCAEL LQLNLVDGII TDDSDVFLFG GTKIYKNMFH EKNYVEFYDA
     ESILKLLGLD RKNMIELAQL LGSDYTNGLK GMGPVSSIEV IAEFGNLKNF KDWYNNGQFD
     KRKQETENKF EKDLRKKLVN NEIILDDDFP SVMVYDAYMR PEVDHDTTPF VWGVPDLDML
     RSFMKTQLGW PHEKSDEILI PLIRDVNKRK KKGKQKRINE FFPREYISGD KKLNTSKRIS
     TATGKLKKRK M
//
ID   RFC1_YEAST              Reviewed;         861 AA.
AC   P38630; D6W2S3;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-NOV-2015, entry version 147.
DE   RecName: Full=Replication factor C subunit 1;
DE            Short=Replication factor C1;
DE   AltName: Full=Activator 1 95 kDa subunit;
DE   AltName: Full=Cell division control protein 44;
GN   Name=RFC1; Synonyms=CDC44; OrderedLocusNames=YOR217W;
GN   ORFNames=YOR50-7;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND MUTAGENESIS OF ASP-427; GLY-436; GLY-512 AND
RP   ASP-513.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8264593;
RA   Howell E.A., McAlear M.A., Rose D., Holm C.;
RT   "CDC44: a putative nucleotide-binding protein required for cell cycle
RT   progression that has homology to subunits of replication factor C.";
RL   Mol. Cell. Biol. 14:255-267(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION IN THE RFC
RP   COMPLEX.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7651383;
RA   Cullmann G., Fien K., Kobayashi R., Stillman B.;
RT   "Characterization of the five replication factor C genes of
RT   Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 15:4661-4671(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8840505;
RX   DOI=10.1002/(SICI)1097-0061(199607)12:9<877::AID-YEA969>3.0.CO;2-S;
RA   Galisson F., Dujon B.;
RT   "Sequence and analysis of a 33 kb fragment from the right arm of
RT   chromosome XV of the yeast Saccharomyces cerevisiae.";
RL   Yeast 12:877-885(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
RA   Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
RA   Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
RA   Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
RA   Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
RA   Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
RA   Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
RA   Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
RA   Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
RA   Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
RA   Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
RA   Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
RA   Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
RA   Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
RA   Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   INTERACTION WITH POL30.
RX   PubMed=14530260; DOI=10.1074/jbc.M309206200;
RA   Yao N., Coryell L., Zhang D., Georgescu R.E., Finkelstein J.,
RA   Coman M.M., Hingorani M.M., O'Donnell M.;
RT   "Replication factor C clamp loader subunit arrangement within the
RT   circular pentamer and its attachment points to proliferating cell
RT   nuclear antigen.";
RL   J. Biol. Chem. 278:50744-50753(2003).
RN   [7]
RP   INTERACTION WITH ECO1.
RX   PubMed=12665596; DOI=10.1128/MCB.23.8.2999-3007.2003;
RA   Kenna M.A., Skibbens R.V.;
RT   "Mechanical link between cohesion establishment and DNA replication:
RT   Ctf7p/Eco1p, a cohesion establishment factor, associates with three
RT   different replication factor C complexes.";
RL   Mol. Cell. Biol. 23:2999-3007(2003).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   IDENTIFICATION IN THE RFC COMPLEX.
RX   PubMed=15964801; DOI=10.1128/MCB.25.13.5445-5455.2005;
RA   Bylund G.O., Burgers P.M.;
RT   "Replication protein A-directed unloading of PCNA by the Ctf18
RT   cohesion establishment complex.";
RL   Mol. Cell. Biol. 25:5445-5455(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38 AND SER-40, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38 AND SER-40, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; SER-40 AND THR-63,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 295-785 IN COMPLEX WITH AN
RP   ATP ANALOG; RCF2; RCF3; RCF4; RCF5 AND PCNA.
RX   PubMed=15201901; DOI=10.1038/nature02585;
RA   Bowman G.D., O'Donnell M., Kuriyan J.;
RT   "Structural analysis of a eukaryotic sliding DNA clamp-clamp loader
RT   complex.";
RL   Nature 429:724-730(2004).
CC   -!- FUNCTION: Component of the ATP-dependent clamp loader RFC complex
CC       for the POL30/PCNA homotrimer DNA clamp. During a clamp loading
CC       circle, the RFC:clamp complex binds to DNA and the recognition of
CC       the double-stranded/single-stranded junction stimulates ATP
CC       hydrolysis by RFC. The complex presumably provides bipartite ATP
CC       sites in which one subunit supplies a catalytic site for
CC       hydrolysis of ATP bound to the neighboring subunit. Dissociation
CC       of RFC from the clamp leaves the clamp encircling DNA. Replication
CC       factor C (RFC or activator 1) complex acts during elongation of
CC       primed DNA templates by DNA polymerase delta and epsilon. RFC has
CC       an essential but redundant activity in sister chromatid cohesion
CC       establishment.
CC   -!- SUBUNIT: Replication factor C (RFC) is a heteropentamer of
CC       subunits RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with
CC       POL30/PCNA in the presence of ATP. Interacts with ECO1 and
CC       POL30/PCNA. {ECO:0000269|PubMed:12665596,
CC       ECO:0000269|PubMed:14530260, ECO:0000269|PubMed:15201901,
CC       ECO:0000269|PubMed:15964801, ECO:0000269|PubMed:7651383}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 BRCT domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00033}.
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DR   EMBL; U03102; AAC48916.1; -; Unassigned_DNA.
DR   EMBL; U26027; AAC49060.1; -; Genomic_DNA.
DR   EMBL; X92441; CAA63180.1; -; Genomic_DNA.
DR   EMBL; Z75125; CAA99434.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10989.1; -; Genomic_DNA.
DR   PIR; S44763; S44763.
DR   RefSeq; NP_014860.1; NM_001183636.1.
DR   PDB; 1SXJ; X-ray; 2.85 A; A=295-785.
DR   PDBsum; 1SXJ; -.
DR   ProteinModelPortal; P38630; -.
DR   SMR; P38630; 151-243, 298-554.
DR   BioGrid; 34612; 61.
DR   DIP; DIP-2527N; -.
DR   IntAct; P38630; 12.
DR   MINT; MINT-619267; -.
DR   MaxQB; P38630; -.
DR   PeptideAtlas; P38630; -.
DR   EnsemblFungi; YOR217W; YOR217W; YOR217W.
DR   GeneID; 854392; -.
DR   KEGG; sce:YOR217W; -.
DR   EuPathDB; FungiDB:YOR217W; -.
DR   SGD; S000005743; RFC1.
DR   GeneTree; ENSGT00730000111066; -.
DR   HOGENOM; HOG000164552; -.
DR   InParanoid; P38630; -.
DR   KO; K10754; -.
DR   OMA; AHSHILA; -.
DR   OrthoDB; EOG7BGHVG; -.
DR   BioCyc; YEAST:G3O-33719-MONOMER; -.
DR   Reactome; R-SCE-109977; Repair synthesis for gap-filling by DNA polymerase in TC-NER.
DR   Reactome; R-SCE-110312; Translesion synthesis by REV1.
DR   Reactome; R-SCE-110320; Translesion Synthesis by POLH.
DR   Reactome; R-SCE-174411; Polymerase switching on the C-strand of the telomere.
DR   Reactome; R-SCE-5655862; Translesion synthesis by POLK.
DR   Reactome; R-SCE-5656121; Translesion synthesis by POLI.
DR   Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-SCE-69091; Polymerase switching.
DR   EvolutionaryTrace; P38630; -.
DR   NextBio; 976553; -.
DR   PRO; PR:P38630; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   GO; GO:0005663; C:DNA replication factor C complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IMP:SGD.
DR   GO; GO:0006272; P:leading strand elongation; IDA:SGD.
DR   GO; GO:0006298; P:mismatch repair; IGI:SGD.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:SGD.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012178; RFC1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF08519; RFC1; 1.
DR   PIRSF; PIRSF036578; RFC1; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50172; BRCT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell cycle; Cell division;
KW   Complete proteome; DNA replication; DNA-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN         1    861       Replication factor C subunit 1.
FT                                /FTId=PRO_0000121776.
FT   DOMAIN      153    243       BRCT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   NP_BIND     353    361       ATP.
FT   MOTIF       830    834       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       855    860       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   BINDING     299    299       ATP; via carbonyl oxygen.
FT   BINDING     311    311       ATP; via amide nitrogen and carbonyl
FT                                oxygen.
FT   BINDING     456    456       ATP.
FT   MOD_RES      38     38       Phosphothreonine.
FT                                {ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES      40     40       Phosphoserine.
FT                                {ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES      63     63       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MUTAGEN     427    427       D->H: In cs mutant CDC44-2; causes cell
FT                                cycle arrest.
FT                                {ECO:0000269|PubMed:8264593}.
FT   MUTAGEN     436    436       G->R: In cs mutant CDC44-3/4; causes cell
FT                                cycle arrest.
FT                                {ECO:0000269|PubMed:8264593}.
FT   MUTAGEN     512    512       G->A: In cs mutant CDC44-9; no effect.
FT                                {ECO:0000269|PubMed:8264593}.
FT   MUTAGEN     513    513       D->N: In cs mutants CDC44-1/5/8 and
FT                                CDC44-9; causes cell cycle arrest.
FT                                {ECO:0000269|PubMed:8264593}.
FT   HELIX       298    301       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       307    309       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       314    325       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       327    332       {ECO:0000244|PDB:1SXJ}.
FT   TURN        333    335       {ECO:0000244|PDB:1SXJ}.
FT   STRAND      347    352       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       359    369       {ECO:0000244|PDB:1SXJ}.
FT   STRAND      373    377       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       385    390       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       392    395       {ECO:0000244|PDB:1SXJ}.
FT   TURN        402    406       {ECO:0000244|PDB:1SXJ}.
FT   STRAND      418    423       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       426    428       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       436    446       {ECO:0000244|PDB:1SXJ}.
FT   STRAND      451    456       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       464    466       {ECO:0000244|PDB:1SXJ}.
FT   TURN        467    469       {ECO:0000244|PDB:1SXJ}.
FT   STRAND      470    474       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       480    493       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       502    509       {ECO:0000244|PDB:1SXJ}.
FT   TURN        510    512       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       514    521       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       523    527       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       535    544       {ECO:0000244|PDB:1SXJ}.
FT   TURN        545    548       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       550    558       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       561    563       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       568    570       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       574    581       {ECO:0000244|PDB:1SXJ}.
FT   TURN        585    587       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       588    595       {ECO:0000244|PDB:1SXJ}.
FT   STRAND      596    602       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       610    631       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       638    640       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       641    648       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       650    654       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       669    687       {ECO:0000244|PDB:1SXJ}.
FT   TURN        688    692       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       699    703       {ECO:0000244|PDB:1SXJ}.
FT   TURN        704    706       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       707    714       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       725    730       {ECO:0000244|PDB:1SXJ}.
FT   TURN        731    733       {ECO:0000244|PDB:1SXJ}.
FT   HELIX       737    746       {ECO:0000244|PDB:1SXJ}.
SQ   SEQUENCE   861 AA;  94903 MW;  A7D9208D66DD9A98 CRC64;
     MVNISDFFGK NKKSVRSSTS RPTRQVGSSK PEVIDLDTES DQESTNKTPK KMPVSNVIDV
     SETPEGEKKL PLPAKRKASS PTVKPASSKK TKPSSKSSDS ASNITAQDVL DKIPSLDLSN
     VHVKENAKFD FKSANSNADP DEIVSEIGSF PEGKPNCLLG LTIVFTGVLP TLERGASEAL
     AKRYGARVTK SISSKTSVVV LGDEAGPKKL EKIKQLKIKA IDEEGFKQLI AGMPAEGGDG
     EAAEKARRKL EEQHNIATKE AELLVKKEEE RSKKLAATRV SGGHLERDNV VREEDKLWTV
     KYAPTNLQQV CGNKGSVMKL KNWLANWENS KKNSFKHAGK DGSGVFRAAM LYGPPGIGKT
     TAAHLVAQEL GYDILEQNAS DVRSKTLLNA GVKNALDNMS VVGYFKHNEE AQNLNGKHFV
     IIMDEVDGMS GGDRGGVGQL AQFCRKTSTP LILICNERNL PKMRPFDRVC LDIQFRRPDA
     NSIKSRLMTI AIREKFKLDP NVIDRLIQTT RGDIRQVINL LSTISTTTKT INHENINEIS
     KAWEKNIALK PFDIAHKMLD GQIYSDIGSR NFTLNDKIAL YFDDFDFTPL MIQENYLSTR
     PSVLKPGQSH LEAVAEAANC ISLGDIVEKK IRSSEQLWSL LPLHAVLSSV YPASKVAGHM
     AGRINFTAWL GQNSKSAKYY RLLQEIHYHT RLGTSTDKIG LRLDYLPTFR KRLLDPFLKQ
     GADAISSVIE VMDDYYLTKE DWDSIMEFFV GPDVTTAIIK KIPATVKSGF TRKYNSMTHP
     VAIYRTGSTI GGGGVGTSTS TPDFEDVVDA DDNPVPADDE ETQDSSTDLK KDKLIKQKAK
     PTKRKTATSK PGGSKKRKTK A
//
ID   RRM3_YEAST              Reviewed;         723 AA.
AC   P38766; D3DKX8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   11-NOV-2015, entry version 130.
DE   RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03177};
DE   AltName: Full=Regulation of Ty1 transposition protein 104;
DE   AltName: Full=rDNA recombination mutation protein 3 {ECO:0000255|HAMAP-Rule:MF_03177};
GN   Name=RRM3 {ECO:0000255|HAMAP-Rule:MF_03177}; Synonyms=RTT104;
GN   OrderedLocusNames=YHR031C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
RA   Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
RA   Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
RA   Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
RA   Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
RA   Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
RA   Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=8293975;
RA   Keil R.L., McWilliams A.D.;
RT   "A gene with specific and global effects on recombination of sequences
RT   from tandemly repeated genes in Saccharomyces cerevisiae.";
RL   Genetics 135:711-718(1993).
RN   [4]
RP   FUNCTION.
RX   PubMed=10693764; DOI=10.1016/S0092-8674(00)80683-2;
RA   Ivessa A.S., Zhou J.-Q., Zakian V.A.;
RT   "The Saccharomyces Pif1p DNA helicase and the highly related Rrm3p
RT   have opposite effects on replication fork progression in ribosomal
RT   DNA.";
RL   Cell 100:479-489(2000).
RN   [5]
RP   FUNCTION.
RX   PubMed=11779788;
RA   Scholes D.T., Banerjee M., Bowen B., Curcio M.J.;
RT   "Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae
RT   have conserved roles in genome maintenance.";
RL   Genetics 159:1449-1465(2001).
RN   [6]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=12050116; DOI=10.1101/gad.982902;
RA   Ivessa A.S., Zhou J.Q., Schulz V.P., Monson E.K., Zakian V.A.;
RT   "Saccharomyces Rrm3p, a 5' to 3' DNA helicase that promotes
RT   replication fork progression through telomeric and subtelomeric DNA.";
RL   Genes Dev. 16:1383-1396(2002).
RN   [7]
RP   INTERACTION WITH POL30, AND MUTAGENESIS OF PHE-41 AND PHE-42.
RX   PubMed=12239216; DOI=10.1074/jbc.M207263200;
RA   Schmidt K.H., Derry K.L., Kolodner R.D.;
RT   "Saccharomyces cerevisiae RRM3, a 5' to 3' DNA helicase, physically
RT   interacts with proliferating cell nuclear antigen.";
RL   J. Biol. Chem. 277:45331-45337(2002).
RN   [8]
RP   FUNCTION.
RX   PubMed=12686542; DOI=10.1074/jbc.M301610200;
RA   Weitao T., Budd M., Hoopes L.L., Campbell J.L.;
RT   "Dna2 helicase/nuclease causes replicative fork stalling and double-
RT   strand breaks in the ribosomal DNA of Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 278:22513-22522(2003).
RN   [9]
RP   FUNCTION.
RX   PubMed=14690605; DOI=10.1016/S1097-2765(03)00456-8;
RA   Ivessa A.S., Lenzmeier B.A., Bessler J.B., Goudsouzian L.K.,
RA   Schnakenberg S.L., Zakian V.A.;
RT   "The Saccharomyces cerevisiae helicase Rrm3p facilitates replication
RT   past nonhistone protein-DNA complexes.";
RL   Mol. Cell 12:1525-1536(2003).
RN   [10]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [11]
RP   FUNCTION.
RX   PubMed=15037547; DOI=10.1101/gad.1154704;
RA   Torres J.Z., Bessler J.B., Zakian V.A.;
RT   "Local chromatin structure at the ribosomal DNA causes replication
RT   fork pausing and genome instability in the absence of the S.
RT   cerevisiae DNA helicase Rrm3p.";
RL   Genes Dev. 18:498-503(2004).
RN   [12]
RP   FUNCTION, AND DOMAIN.
RX   PubMed=15579680; DOI=10.1534/genetics.104.028035;
RA   Bessler J.B., Zakian V.A.;
RT   "The amino terminus of the Saccharomyces cerevisiae DNA helicase Rrm3p
RT   modulates protein function altering replication and checkpoint
RT   activity.";
RL   Genetics 168:1205-1218(2004).
RN   [13]
RP   FUNCTION.
RX   PubMed=15060144; DOI=10.1128/MCB.24.8.3198-3212.2004;
RA   Torres J.Z., Schnakenberg S.L., Zakian V.A.;
RT   "Saccharomyces cerevisiae Rrm3p DNA helicase promotes genome integrity
RT   by preventing replication fork stalling: viability of rrm3 cells
RT   requires the intra-S-phase checkpoint and fork restart activities.";
RL   Mol. Cell. Biol. 24:3198-3212(2004).
RN   [14]
RP   FUNCTION.
RX   PubMed=15060145; DOI=10.1128/MCB.24.8.3213-3226.2004;
RA   Schmidt K.H., Kolodner R.D.;
RT   "Requirement of Rrm3 helicase for repair of spontaneous DNA lesions in
RT   cells lacking Srs2 or Sgs1 helicase.";
RL   Mol. Cell. Biol. 24:3213-3226(2004).
RN   [15]
RP   FUNCTION.
RX   PubMed=15082794; DOI=10.1128/MCB.24.9.4019-4031.2004;
RA   Makovets S., Herskowitz I., Blackburn E.H.;
RT   "Anatomy and dynamics of DNA replication fork movement in yeast
RT   telomeric regions.";
RL   Mol. Cell. Biol. 24:4019-4031(2004).
RN   [16]
RP   FUNCTION.
RX   PubMed=15542831; DOI=10.1128/MCB.24.23.10208-10222.2004;
RA   Gibson D.G., Aparicio J.G., Hu F., Aparicio O.M.;
RT   "Diminished S-phase cyclin-dependent kinase function elicits vital
RT   Rad53-dependent checkpoint responses in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 24:10208-10222(2004).
RN   [17]
RP   FUNCTION.
RX   PubMed=15775982; DOI=10.1038/sj.emboj.7600602;
RA   Prado F., Aguilera A.;
RT   "Impairment of replication fork progression mediates RNA polII
RT   transcription-associated recombination.";
RL   EMBO J. 24:1267-1276(2005).
RN   [18]
RP   FUNCTION.
RX   PubMed=15907372; DOI=10.1016/j.gene.2005.03.031;
RA   O'Rourke T.W., Doudican N.A., Zhang H., Eaton J.S., Doetsch P.W.,
RA   Shadel G.S.;
RT   "Differential involvement of the related DNA helicases Pif1p and Rrm3p
RT   in mtDNA point mutagenesis and stability.";
RL   Gene 354:86-92(2005).
RN   [19]
RP   RECRUITMENT TO PAUSED REPLISOME.
RX   PubMed=16103218; DOI=10.1101/gad.337205;
RA   Calzada A., Hodgson B., Kanemaki M., Bueno A., Labib K.;
RT   "Molecular anatomy and regulation of a stable replisome at a paused
RT   eukaryotic DNA replication fork.";
RL   Genes Dev. 19:1905-1919(2005).
RN   [20]
RP   INTERACTION WITH DEF1.
RX   PubMed=15863512; DOI=10.1074/jbc.M413562200;
RA   Chen Y.B., Yang C.P., Li R.X., Zeng R., Zhou J.Q.;
RT   "Def1p is involved in telomere maintenance in budding yeast.";
RL   J. Biol. Chem. 280:24784-24791(2005).
RN   [21]
RP   FUNCTION.
RX   PubMed=15829566; DOI=10.1091/mbc.E05-01-0053;
RA   Taylor S.D., Zhang H., Eaton J.S., Rodeheffer M.S., Lebedeva M.A.,
RA   O'rourke T.W., Siede W., Shadel G.S.;
RT   "The conserved Mec1/Rad53 nuclear checkpoint pathway regulates
RT   mitochondrial DNA copy number in Saccharomyces cerevisiae.";
RL   Mol. Biol. Cell 16:3010-3018(2005).
RN   [22]
RP   FUNCTION.
RX   PubMed=16137624; DOI=10.1016/j.molcel.2005.06.037;
RA   Szyjka S.J., Viggiani C.J., Aparicio O.M.;
RT   "Mrc1 is required for normal progression of replication forks
RT   throughout chromatin in S. cerevisiae.";
RL   Mol. Cell 19:691-697(2005).
RN   [23]
RP   FUNCTION.
RX   PubMed=16327883; DOI=10.1371/journal.pgen.0010061;
RA   Budd M.E., Tong A.H., Polaczek P., Peng X., Boone C., Campbell J.L.;
RT   "A network of multi-tasking proteins at the DNA replication fork
RT   preserves genome stability.";
RL   PLoS Genet. 1:E61-E61(2005).
RN   [24]
RP   FUNCTION.
RX   PubMed=16631586; DOI=10.1016/j.cub.2006.02.071;
RA   Luke B., Versini G., Jaquenoud M., Zaidi I.W., Kurz T., Pintard L.,
RA   Pasero P., Peter M.;
RT   "The cullin Rtt101p promotes replication fork progression through
RT   damaged DNA and natural pause sites.";
RL   Curr. Biol. 16:786-792(2006).
RN   [25]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=17114583; DOI=10.1101/gad.1478906;
RA   Azvolinsky A., Dunaway S., Torres J.Z., Bessler J.B., Zakian V.A.;
RT   "The S. cerevisiae Rrm3p DNA helicase moves with the replication fork
RT   and affects replication of all yeast chromosomes.";
RL   Genes Dev. 20:3104-3116(2006).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [27]
RP   FUNCTION.
RX   PubMed=19168400; DOI=10.1016/j.dnarep.2008.12.010;
RA   de la Loza M.C., Wellinger R.E., Aguilera A.;
RT   "Stimulation of direct-repeat recombination by RNA polymerase III
RT   transcription.";
RL   DNA Repair 8:620-626(2009).
RN   [28]
RP   FUNCTION.
RX   PubMed=19414561; DOI=10.1534/genetics.109.104208;
RA   Stamenova R., Maxwell P.H., Kenny A.E., Curcio M.J.;
RT   "Rrm3 protects the Saccharomyces cerevisiae genome from instability at
RT   nascent sites of retrotransposition.";
RL   Genetics 182:711-723(2009).
RN   [29]
RP   FUNCTION.
RX   PubMed=21087929; DOI=10.1074/jbc.M110.189456;
RA   Bairwa N.K., Mohanty B.K., Stamenova R., Curcio M.J., Bastia D.;
RT   "The intra-S phase checkpoint protein Tof1 collaborates with the
RT   helicase Rrm3 and the F-box protein Dia2 to maintain genome stability
RT   in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 286:2445-2454(2011).
RN   [30]
RP   FUNCTION.
RX   PubMed=21172804; DOI=10.1242/jcs.077313;
RA   Hashash N., Johnson A.L., Cha R.S.;
RT   "Regulation of fragile sites expression in budding yeast by MEC1, RRM3
RT   and hydroxyurea.";
RL   J. Cell Sci. 124:181-185(2011).
RN   [31]
RP   FUNCTION IN G4-UNWINDING.
RX   PubMed=23657261; DOI=10.1038/nature12149;
RA   Paeschke K., Bochman M.L., Garcia P.D., Cejka P., Friedman K.L.,
RA   Kowalczykowski S.C., Zakian V.A.;
RT   "Pif1 family helicases suppress genome instability at G-quadruplex
RT   motifs.";
RL   Nature 497:458-462(2013).
CC   -!- FUNCTION: 5' to 3' DNA replicative helicase recruited to paused
CC       replisomes to promote fork progression throughout nonhistone
CC       protein-DNA complexes, naturally occurring impediments that are
CC       encountered in each S phase where replication forks pauses. Needed
CC       for normal fork progression through over 1000 discrete sites
CC       scattered throughout the genome, like rDNA, tRNA genes,
CC       centromeres, active replication origins, or transcriptional
CC       silencers. Required for timely replication of the telomere and
CC       subtelomeric DNA and for wild-type levels of telomeric silencing.
CC       Involved in regulation of Ty1 transposition and protects the
CC       genome from instability at nascent sites of retrotransposition.
CC       Involved in DNA repair during stalled replication fork, regulation
CC       of fragile sites expression and essential for genome stability.
CC       Plays also a role in mtDNA replication. Has G-quadruplex (G4)
CC       unwinding activity and can suppress G4-induced genome instability
CC       when PIF1 levels are low. {ECO:0000269|PubMed:10693764,
CC       ECO:0000269|PubMed:11779788, ECO:0000269|PubMed:12050116,
CC       ECO:0000269|PubMed:12686542, ECO:0000269|PubMed:14690605,
CC       ECO:0000269|PubMed:15037547, ECO:0000269|PubMed:15060144,
CC       ECO:0000269|PubMed:15060145, ECO:0000269|PubMed:15082794,
CC       ECO:0000269|PubMed:15542831, ECO:0000269|PubMed:15579680,
CC       ECO:0000269|PubMed:15775982, ECO:0000269|PubMed:15829566,
CC       ECO:0000269|PubMed:15907372, ECO:0000269|PubMed:16137624,
CC       ECO:0000269|PubMed:16327883, ECO:0000269|PubMed:16631586,
CC       ECO:0000269|PubMed:17114583, ECO:0000269|PubMed:19168400,
CC       ECO:0000269|PubMed:19414561, ECO:0000269|PubMed:21087929,
CC       ECO:0000269|PubMed:21172804, ECO:0000269|PubMed:23657261,
CC       ECO:0000269|PubMed:8293975}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_03177}.
CC   -!- SUBUNIT: Interacts with DEF1 and POL30.
CC       {ECO:0000269|PubMed:12239216, ECO:0000269|PubMed:15863512}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere.
CC   -!- DOMAIN: The N-terminal part (residues 1 to 249) is essential for
CC       function and confers locus specificity.
CC       {ECO:0000269|PubMed:15579680}.
CC   -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR   EMBL; U00062; AAB68913.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06722.1; -; Genomic_DNA.
DR   PIR; S46744; S46744.
DR   RefSeq; NP_011896.1; NM_001179161.1.
DR   ProteinModelPortal; P38766; -.
DR   BioGrid; 36462; 156.
DR   DIP; DIP-2858N; -.
DR   IntAct; P38766; 4.
DR   MINT; MINT-1556551; -.
DR   MaxQB; P38766; -.
DR   PRIDE; P38766; -.
DR   EnsemblFungi; YHR031C; YHR031C; YHR031C.
DR   GeneID; 856426; -.
DR   KEGG; sce:YHR031C; -.
DR   EuPathDB; FungiDB:YHR031C; -.
DR   SGD; S000001073; RRM3.
DR   GeneTree; ENSGT00530000063561; -.
DR   HOGENOM; HOG000132960; -.
DR   InParanoid; P38766; -.
DR   KO; K15255; -.
DR   OMA; TESEWAD; -.
DR   OrthoDB; EOG76MKKK; -.
DR   BioCyc; YEAST:G3O-31091-MONOMER; -.
DR   NextBio; 982006; -.
DR   PRO; PR:P38766; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   GO; GO:0005724; C:nuclear telomeric heterochromatin; IPI:SGD.
DR   GO; GO:0005657; C:replication fork; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IMP:SGD.
DR   GO; GO:0032508; P:DNA duplex unwinding; IDA:GOC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IMP:SGD.
DR   GO; GO:0044806; P:G-quadruplex DNA unwinding; IMP:SGD.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IGI:SGD.
DR   GO; GO:0097046; P:replication fork progression beyond termination site; IMP:SGD.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 3.
DR   HAMAP; MF_03176; PIF1; 1.
DR   HAMAP; MF_03177; RRM3; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003840; DNA_helicase.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR028880; Rrm3.
DR   PANTHER; PTHR23274; PTHR23274; 2.
DR   Pfam; PF05970; PIF1; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
PE   1: Evidence at protein level;
KW   ATP-binding; Chromosome; Complete proteome; DNA damage; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Telomere.
FT   CHAIN         1    723       ATP-dependent DNA helicase RRM3.
FT                                /FTId=PRO_0000101986.
FT   NP_BIND     254    261       ATP. {ECO:0000255|HAMAP-Rule:MF_03177}.
FT   DNA_BIND    682    701       {ECO:0000255|HAMAP-Rule:MF_03177}.
FT   MOD_RES      64     64       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   MUTAGEN      41     41       F->A,D: Reduces the interaction with
FT                                POL30; when associated with A-42 or D-42.
FT                                {ECO:0000269|PubMed:12239216}.
FT   MUTAGEN      42     42       F->A,D: Reduces the interaction with
FT                                POL30; when associated with A-42 or D-42.
FT                                {ECO:0000269|PubMed:12239216}.
SQ   SEQUENCE   723 AA;  81581 MW;  8E0010ABB870CAB6 CRC64;
     MFRSHASGNK KQWSKRSSNG STPAASASGS HAYRQQTLSS FFMGCGKKSA AASKNSTTII
     DLESGDEGNR NITAPPRPRL IRNNSSSLFS QSQGSFGDDD PDAEFKKLVD VPRLNSYKKS
     SRSLSMTSSL HKTASASTTQ KTYHFDEDET LREVTSVKSN SRQLSFTSTI NIEDSSMKLS
     TDSERPAKRS KPSMEFQGLK LTVPKKIKPL LRKTVSNMDS MNHRSASSPV VLTMEQERVV
     NLIVKKRTNV FYTGSAGTGK SVILQTIIRQ LSSLYGKESI AITASTGLAA VTIGGSTLHK
     WSGIGIGNKT IDQLVKKIQS QKDLLAAWRY TKVLIIDEIS MVDGNLLDKL EQIARRIRKN
     DDPFGGIQLV LTGDFFQLPP VAKKDEHNVV KFCFESEMWK RCIQKTILLT KVFRQQDNKL
     IDILNAIRYG ELTVDIAKTI RNLNRDIDYA DGIAPTELYA TRREVELSNV KKLQSLPGDL
     YEFKAVDNAP ERYQAILDSS LMVEKVVALK EDAQVMMLKN KPDVELVNGS LGKVLFFVTE
     SLVVKMKEIY KIVDDEVVMD MRLVSRVIGN PLLKESKEFR QDLNARPLAR LERLKILINY
     AVKISPHKEK FPYVRWTVGK NKYIHELMVP ERFPIDIPRE NVGLERTQIP LMLCWALSIH
     KAQGQTIQRL KVDLRRIFEA GQVYVALSRA VTMDTLQVLN FDPGKIRTNE RVKDFYKRLE
     TLK
//
ID   UNG_HUMAN               Reviewed;         313 AA.
AC   P13051; A8K5M6; B2R8Y1; O00637; O00719; Q93028;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 2.
DT   11-NOV-2015, entry version 179.
DE   RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166};
DE            Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166};
DE            EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
GN   Name=UNG {ECO:0000255|HAMAP-Rule:MF_03166};
GN   Synonyms=DGU, UNG1 {ECO:0000255|HAMAP-Rule:MF_03166},
GN   UNG15 {ECO:0000255|HAMAP-Rule:MF_03166};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF
RP   87-113.
RC   TISSUE=Placenta;
RX   PubMed=2555154;
RA   Olsen L.C., Aasland R., Wittwer C.U., Krokan H.E., Helland D.E.;
RT   "Molecular cloning of human uracil-DNA glycosylase, a highly conserved
RT   DNA repair enzyme.";
RL   EMBO J. 8:3121-3125(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7926048; DOI=10.1016/0014-5793(94)01042-0;
RA   Haug T., Skorpen F., Lund H., Krokan H.E.;
RT   "Structure of the gene for human uracil-DNA glycosylase and analysis
RT   of the promoter function.";
RL   FEBS Lett. 353:180-184(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND ALTERNATIVE
RP   SPLICING.
RX   PubMed=9016624; DOI=10.1093/nar/25.4.750;
RA   Nilsen H., Solum K., Haug T., Krokan H.E.;
RT   "Nuclear and mitochondrial uracil-DNA glycosylases are generated by
RT   alternative splicing and transcription from different positions in the
RT   UNG gene.";
RL   Nucleic Acids Res. 25:750-755(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8332455; DOI=10.1093/nar/21.11.2579;
RA   Slupphaug G., Markussen F.-H., Olsen L.C., Aasland R., Aarsaether N.,
RA   Bakke O., Krokan H.E., Helland D.E.;
RT   "Nuclear and mitochondrial forms of human uracil-DNA glycosylase are
RT   encoded by the same gene.";
RL   Nucleic Acids Res. 21:2579-2584(1993).
RN   [9]
RP   MUTAGENESIS.
RX   PubMed=8670846;
RA   Kavli B., Slupphaug G., Mol C.D., Arvai A.S., Petersen S.B.,
RA   Tainer J.A., Krohan H.E.;
RT   "Excision of cytosine and thymine from DNA by mutants of human uracil-
RT   DNA glycosylase.";
RL   EMBO J. 15:3442-3447(1996).
RN   [10]
RP   INTERACTION WITH HIV-1 VPR.
RX   PubMed=8551605;
RA   Bouhamdan M., Benichou S., Rey F., Navarro J.-M., Agostini I.,
RA   Spire B., Camonis J., Slupphaug G., Vigne R., Benarous R., Sire J.;
RT   "Human immunodeficiency virus type 1 Vpr protein binds to the uracil
RT   DNA glycosylase DNA repair enzyme.";
RL   J. Virol. 70:697-704(1996).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9753728; DOI=10.1093/nar/26.20.4611;
RA   Otterlei M., Haug T., Nagelhus T.A., Slupphaug G., Lindmo T.,
RA   Krokan H.E.;
RT   "Nuclear and mitochondrial splice forms of human uracil-DNA
RT   glycosylase contain a complex nuclear localisation signal and a strong
RT   classical mitochondrial localisation signal, respectively.";
RL   Nucleic Acids Res. 26:4611-4617(1998).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [13]
RP   INTERACTION WITH FAM72A.
RX   PubMed=18676834; DOI=10.1158/0008-5472.CAN-08-1259;
RA   Guo C., Zhang X., Fink S.P., Platzer P., Wilson K., Willson J.K.,
RA   Wang Z., Markowitz S.D.;
RT   "Ugene, a newly identified protein that is commonly overexpressed in
RT   cancer and binds uracil DNA glycosylase.";
RL   Cancer Res. 68:6118-6126(2008).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-14; SER-23;
RP   THR-60 AND SER-64, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-23; THR-60 AND
RP   SER-64, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-295, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-14; SER-23 AND
RP   THR-60, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND THR-60, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=7697717; DOI=10.1016/0092-8674(95)90290-2;
RA   Mol C.D., Arvai A.S., Slupphaug G., Kavli B., Alseth I., Krohan H.E.,
RA   Tainer J.A.;
RT   "Crystal structure and mutational analysis of human uracil-DNA
RT   glycosylase: structural basis for specificity and catalysis.";
RL   Cell 80:869-878(1995).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=7671300; DOI=10.1016/0092-8674(95)90467-0;
RA   Mol C.D., Arvai A.S., Sanderson R.J., Slupphaug G., Kavli B.,
RA   Krokan H.E., Mosbaugh D.W., Tainer J.A.;
RT   "Crystal structure of human uracil-DNA glycosylase in complex with a
RT   protein inhibitor: protein mimicry of DNA.";
RL   Cell 82:701-708(1995).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX   PubMed=8900285; DOI=10.1038/384087a0;
RA   Slupphaug G., Mol C.D., Kavli B., Arvai A.S., Krohan H.E.,
RA   Tainer J.A.;
RT   "A nucleotide-flipping mechanism from the structure of human uracil-
RT   DNA glycosylase bound to DNA.";
RL   Nature 384:87-92(1996).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 94-313.
RX   PubMed=9724657; DOI=10.1093/emboj/17.17.5214;
RA   Parikh S.S., Mol C.D., Slupphaug G., Bharati S., Krokan H.E.,
RA   Tainer J.A.;
RT   "Base excision repair initiation revealed by crystal structures and
RT   binding kinetics of human uracil-DNA glycosylase with DNA.";
RL   EMBO J. 17:5214-5226(1998).
RN   [25]
RP   VARIANT HIGM5 SER-251.
RX   PubMed=12958596; DOI=10.1038/ni974;
RA   Imai K., Slupphaug G., Lee W.-I., Revy P., Nonoyama S., Catalan N.,
RA   Yel L., Forveille M., Kavli B., Krokan H.E., Ochs H.D., Fischer A.,
RA   Durandy A.;
RT   "Human uracil-DNA glycosylase deficiency associated with profoundly
RT   impaired immunoglobulin class-switch recombination.";
RL   Nat. Immunol. 4:1023-1028(2003).
RN   [26]
RP   CHARACTERIZATION OF VARIANT HIGM5 SER-251.
RX   PubMed=15967827; DOI=10.1084/jem.20050042;
RA   Kavli B., Andersen S., Otterlei M., Liabakk N.B., Imai K., Fischer A.,
RA   Durandy A., Krokan H.E., Slupphaug G.;
RT   "B cells from hyper-IgM patients carrying UNG mutations lack ability
RT   to remove uracil from ssDNA and have elevated genomic uracil.";
RL   J. Exp. Med. 201:2011-2021(2005).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as
CC       a result of misincorporation of dUMP residues by DNA polymerase or
CC       due to deamination of cytosine.
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes single-stranded DNA or mismatched
CC       double-stranded DNA and polynucleotides, releasing free uracil.
CC       {ECO:0000255|HAMAP-Rule:MF_03166}.
CC   -!- SUBUNIT: Monomer. Interacts with FAM72A. Interacts with HIV-1 Vpr.
CC       {ECO:0000255|HAMAP-Rule:MF_03166, ECO:0000269|PubMed:18676834,
CC       ECO:0000269|PubMed:8551605}.
CC   -!- INTERACTION:
CC       P15927:RPA2; NbExp=6; IntAct=EBI-1025947, EBI-621404;
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=UNG2;
CC         IsoId=P13051-1; Sequence=Displayed;
CC       Name=1; Synonyms=UNG1;
CC         IsoId=P13051-2; Sequence=VSP_008513;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed with the highest
CC       expression in skeletal muscle, heart and testicles. Isoform 2 has
CC       the highest expression levels in tissues containing proliferating
CC       cells.
CC   -!- PTM: Isoform 1 is processed by cleavage of a transit peptide.
CC   -!- DISEASE: Immunodeficiency with hyper-IgM 5 (HIGM5) [MIM:608106]: A
CC       rare immunodeficiency syndrome characterized by normal or elevated
CC       serum IgM levels with absence of IgG, IgA, and IgE. It results in
CC       a profound susceptibility to bacterial infections.
CC       {ECO:0000269|PubMed:12958596}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03166}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ung/";
CC   -!- WEB RESOURCE: Name=UNGbase; Note=UNG mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/UNGbase/";
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DR   EMBL; X15653; CAA33679.1; -; mRNA.
DR   EMBL; X89398; CAA61578.1; -; Genomic_DNA.
DR   EMBL; X89398; CAA61579.1; -; Genomic_DNA.
DR   EMBL; Y09008; CAA70211.1; -; mRNA.
DR   EMBL; AF526277; AAM77695.1; -; Genomic_DNA.
DR   EMBL; AK291341; BAF84030.1; -; mRNA.
DR   EMBL; AK313552; BAG36328.1; -; mRNA.
DR   EMBL; CH471054; EAW97846.1; -; Genomic_DNA.
DR   EMBL; CH471054; EAW97847.1; -; Genomic_DNA.
DR   EMBL; BC015205; AAH15205.1; -; mRNA.
DR   EMBL; BC050634; AAH50634.1; -; mRNA.
DR   CCDS; CCDS9124.1; -. [P13051-1]
DR   CCDS; CCDS9125.1; -. [P13051-2]
DR   PIR; S05964; A60472.
DR   RefSeq; NP_003353.1; NM_003362.3. [P13051-2]
DR   RefSeq; NP_550433.1; NM_080911.2. [P13051-1]
DR   UniGene; Hs.191334; -.
DR   PDB; 1AKZ; X-ray; 1.57 A; A=94-313.
DR   PDB; 1DPU; NMR; -; B=73-88.
DR   PDB; 1EMH; X-ray; 1.80 A; A=94-313.
DR   PDB; 1EMJ; X-ray; 2.00 A; A=94-313.
DR   PDB; 1Q3F; X-ray; 1.90 A; A=94-313.
DR   PDB; 1SSP; X-ray; 1.90 A; E=94-313.
DR   PDB; 1UGH; X-ray; 1.90 A; E=94-313.
DR   PDB; 1YUO; X-ray; 1.95 A; A=91-313.
DR   PDB; 2HXM; X-ray; 1.30 A; A=94-313.
DR   PDB; 2OXM; X-ray; 2.50 A; A=94-313.
DR   PDB; 2OYT; X-ray; 2.00 A; A=94-313.
DR   PDB; 2SSP; X-ray; 2.25 A; E=94-313.
DR   PDB; 3FCF; X-ray; 1.84 A; A=94-313.
DR   PDB; 3FCI; X-ray; 1.27 A; A=94-313.
DR   PDB; 3FCK; X-ray; 1.64 A; B=94-313.
DR   PDB; 3FCL; X-ray; 1.70 A; A/B=94-313.
DR   PDB; 3TKB; X-ray; 1.50 A; A=94-313.
DR   PDB; 4SKN; X-ray; 2.90 A; E=94-313.
DR   PDBsum; 1AKZ; -.
DR   PDBsum; 1DPU; -.
DR   PDBsum; 1EMH; -.
DR   PDBsum; 1EMJ; -.
DR   PDBsum; 1Q3F; -.
DR   PDBsum; 1SSP; -.
DR   PDBsum; 1UGH; -.
DR   PDBsum; 1YUO; -.
DR   PDBsum; 2HXM; -.
DR   PDBsum; 2OXM; -.
DR   PDBsum; 2OYT; -.
DR   PDBsum; 2SSP; -.
DR   PDBsum; 3FCF; -.
DR   PDBsum; 3FCI; -.
DR   PDBsum; 3FCK; -.
DR   PDBsum; 3FCL; -.
DR   PDBsum; 3TKB; -.
DR   PDBsum; 4SKN; -.
DR   ProteinModelPortal; P13051; -.
DR   SMR; P13051; 94-313.
DR   BioGrid; 113220; 15.
DR   DIP; DIP-24194N; -.
DR   IntAct; P13051; 9.
DR   MINT; MINT-1507980; -.
DR   STRING; 9606.ENSP00000242576; -.
DR   BindingDB; P13051; -.
DR   ChEMBL; CHEMBL3277; -.
DR   PhosphoSite; P13051; -.
DR   BioMuta; UNG; -.
DR   DMDM; 37999897; -.
DR   MaxQB; P13051; -.
DR   PaxDb; P13051; -.
DR   PRIDE; P13051; -.
DR   DNASU; 7374; -.
DR   Ensembl; ENST00000242576; ENSP00000242576; ENSG00000076248. [P13051-1]
DR   Ensembl; ENST00000336865; ENSP00000337398; ENSG00000076248. [P13051-2]
DR   GeneID; 7374; -.
DR   KEGG; hsa:7374; -.
DR   UCSC; uc001tnz.2; human. [P13051-1]
DR   CTD; 7374; -.
DR   GeneCards; UNG; -.
DR   HGNC; HGNC:12572; UNG.
DR   HPA; CAB011605; -.
DR   MIM; 191525; gene.
DR   MIM; 608106; phenotype.
DR   neXtProt; NX_P13051; -.
DR   Orphanet; 101092; Hyper-IgM syndrome type 5.
DR   PharmGKB; PA364; -.
DR   eggNOG; KOG2994; Eukaryota.
DR   eggNOG; COG0692; LUCA.
DR   GeneTree; ENSGT00390000003405; -.
DR   HOGENOM; HOG000229528; -.
DR   HOVERGEN; HBG000396; -.
DR   InParanoid; P13051; -.
DR   KO; K03648; -.
DR   OMA; YPAPKNI; -.
DR   OrthoDB; EOG786H4X; -.
DR   PhylomeDB; P13051; -.
DR   TreeFam; TF315028; -.
DR   BRENDA; 3.2.2.27; 2681.
DR   Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
DR   Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
DR   Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1.
DR   SABIO-RK; P13051; -.
DR   ChiTaRS; UNG; human.
DR   EvolutionaryTrace; P13051; -.
DR   GeneWiki; Uracil-DNA_glycosylase; -.
DR   GenomeRNAi; 7374; -.
DR   NextBio; 28874; -.
DR   PRO; PR:P13051; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; P13051; -.
DR   CleanEx; HS_UNG; -.
DR   ExpressionAtlas; P13051; baseline and differential.
DR   Genevisible; P13051; HS.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR   GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; NAS:UniProtKB.
DR   GO; GO:0006284; P:base-excision repair; TAS:Reactome.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IDA:UniProtKB.
DR   GO; GO:0045008; P:depyrimidination; TAS:Reactome.
DR   GO; GO:0006281; P:DNA repair; TAS:Reactome.
DR   GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IEA:Ensembl.
DR   GO; GO:0016447; P:somatic recombination of immunoglobulin gene segments; IEA:Ensembl.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.470.10; -; 1.
DR   HAMAP; MF_00148; UDG; 1.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR002043; Ura_DNA_glycsylse.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   PANTHER; PTHR11264; PTHR11264; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   TIGRFAMs; TIGR00628; ung; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   Direct protein sequencing; Disease mutation; DNA damage; DNA repair;
KW   Glycosidase; Host-virus interaction; Hydrolase; Mitochondrion;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN         1    313       Uracil-DNA glycosylase.
FT                                /FTId=PRO_0000176173.
FT   REGION        1     25       FAM72A-binding.
FT   ACT_SITE    154    154       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03166}.
FT   MOD_RES      12     12       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES      14     14       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES      23     23       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES      60     60       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES      64     64       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332}.
FT   MOD_RES     295    295       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   VAR_SEQ       1     44       MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESG
FT                                DAA -> MGVFCLGPWGLGRKLRTPGKGPLQLLSRLCGDHL
FT                                Q (in isoform 1).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:2555154}.
FT                                /FTId=VSP_008513.
FT   VARIANT       4      4       Q -> R (in dbSNP:rs7488798).
FT                                /FTId=VAR_052697.
FT   VARIANT     251    251       F -> S (in HIGM5; fully active and stable
FT                                when expressed in E.coli; mistargeted to
FT                                mitochondria rather than the nucleus).
FT                                {ECO:0000269|PubMed:12958596,
FT                                ECO:0000269|PubMed:15967827}.
FT                                /FTId=VAR_017094.
FT   MUTAGEN     154    154       D->E,N: Loss of activity.
FT                                {ECO:0000269|PubMed:8670846}.
FT   MUTAGEN     156    156       Y->A,C,S: Thymine-DNA glycosylase
FT                                activity. {ECO:0000269|PubMed:8670846}.
FT   MUTAGEN     213    213       N->D: Cytosine-DNA glycosylase activity.
FT                                {ECO:0000269|PubMed:8670846}.
FT   HELIX        77     86       {ECO:0000244|PDB:1DPU}.
FT   HELIX        96    102       {ECO:0000244|PDB:3FCI}.
FT   HELIX       103    105       {ECO:0000244|PDB:3FCI}.
FT   HELIX       109    124       {ECO:0000244|PDB:3FCI}.
FT   STRAND      127    129       {ECO:0000244|PDB:3FCI}.
FT   HELIX       131    133       {ECO:0000244|PDB:3FCI}.
FT   HELIX       136    138       {ECO:0000244|PDB:3FCI}.
FT   STRAND      139    141       {ECO:0000244|PDB:1EMH}.
FT   HELIX       143    145       {ECO:0000244|PDB:3FCI}.
FT   STRAND      148    152       {ECO:0000244|PDB:3FCI}.
FT   TURN        159    161       {ECO:0000244|PDB:3FCI}.
FT   STRAND      163    165       {ECO:0000244|PDB:3FCK}.
FT   HELIX       177    189       {ECO:0000244|PDB:3FCI}.
FT   TURN        190    192       {ECO:0000244|PDB:3TKB}.
FT   HELIX       202    205       {ECO:0000244|PDB:3FCI}.
FT   TURN        206    208       {ECO:0000244|PDB:3FCI}.
FT   STRAND      209    215       {ECO:0000244|PDB:3FCI}.
FT   TURN        223    228       {ECO:0000244|PDB:3FCI}.
FT   HELIX       231    245       {ECO:0000244|PDB:3FCI}.
FT   STRAND      250    255       {ECO:0000244|PDB:3FCI}.
FT   HELIX       256    261       {ECO:0000244|PDB:3FCI}.
FT   TURN        262    264       {ECO:0000244|PDB:3FCI}.
FT   TURN        267    269       {ECO:0000244|PDB:3FCI}.
FT   STRAND      270    275       {ECO:0000244|PDB:3FCI}.
FT   TURN        280    282       {ECO:0000244|PDB:3FCI}.
FT   HELIX       283    285       {ECO:0000244|PDB:3FCI}.
FT   TURN        286    289       {ECO:0000244|PDB:3FCI}.
FT   HELIX       292    302       {ECO:0000244|PDB:3FCI}.
SQ   SEQUENCE   313 AA;  34645 MW;  A4B27E6198AFE9C0 CRC64;
     MIGQKTLYSF FSPSPARKRH APSPEPAVQG TGVAGVPEES GDAAAIPAKK APAGQEEPGT
     PPSSPLSAEQ LDRIQRNKAA ALLRLAARNV PVGFGESWKK HLSGEFGKPY FIKLMGFVAE
     ERKHYTVYPP PHQVFTWTQM CDIKDVKVVI LGQDPYHGPN QAHGLCFSVQ RPVPPPPSLE
     NIYKELSTDI EDFVHPGHGD LSGWAKQGVL LLNAVLTVRA HQANSHKERG WEQFTDAVVS
     WLNQNSNGLV FLLWGSYAQK KGSAIDRKRH HVLQTAHPSP LSVYRGFFGC RHFSKTNELL
     QKSGKKPIDW KEL
//
ID   UNG_YEAST               Reviewed;         359 AA.
AC   P12887; D6VZF3; E9P912;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   11-NOV-2015, entry version 135.
DE   RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166};
DE            Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166};
DE            EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
DE   Flags: Precursor;
GN   Name=UNG1 {ECO:0000255|HAMAP-Rule:MF_03166};
GN   OrderedLocusNames=YML021C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=2644266;
RA   Percival K.J., Klein M.B., Burgers P.M.J.;
RT   "Molecular cloning and primary structure of the uracil-DNA glycosylase
RT   gene from Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 264:2593-2598(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
RA   Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA   Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   XIII.";
RL   Nature 387:90-93(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 204626 / S288c / A364A;
RX   PubMed=7031606; DOI=10.1093/nar/9.21.5797;
RA   Crosby B., Prakash L., Davis H., Hinkle D.C.;
RT   "Purification and characterization of a uracil-DNA glycosylase from
RT   the yeast, Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 9:5797-5809(1981).
RN   [6]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=1938887;
RA   Impellizzeri K.J., Anderson B., Burgers P.M.;
RT   "The spectrum of spontaneous mutations in a Saccharomyces cerevisiae
RT   uracil-DNA-glycosylase mutant limits the function of this enzyme to
RT   cytosine deamination repair.";
RL   J. Bacteriol. 173:6807-6810(1991).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11812822; DOI=10.1093/nar/29.24.4935;
RA   Chatterjee A., Singh K.K.;
RT   "Uracil-DNA glycosylase-deficient yeast exhibit a mitochondrial
RT   mutator phenotype.";
RL   Nucleic Acids Res. 29:4935-4940(2001).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   INDUCTION.
RX   PubMed=17934734; DOI=10.1007/s00294-007-0159-5;
RA   Lucaccioni A., Pavlov Y.I., Achilli A., Babudri N.;
RT   "High rate of starvation-associated mutagenesis in Ung(-) yeast caused
RT   by the overproduction of human activation-induced deaminase.";
RL   Curr. Genet. 52:239-245(2007).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as
CC       a result of misincorporation of dUMP residues by DNA polymerase or
CC       due to deamination of cytosine. Not involved in strand-directed
CC       mismatch repair. {ECO:0000255|HAMAP-Rule:MF_03166,
CC       ECO:0000269|PubMed:11812822, ECO:0000269|PubMed:1938887,
CC       ECO:0000269|PubMed:2644266, ECO:0000269|PubMed:7031606}.
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes single-stranded DNA or mismatched
CC       double-stranded DNA and polynucleotides, releasing free uracil.
CC       {ECO:0000255|HAMAP-Rule:MF_03166, ECO:0000269|PubMed:7031606}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5-8. {ECO:0000269|PubMed:7031606};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-
CC       Rule:MF_03166, ECO:0000269|PubMed:11812822}. Nucleus
CC       {ECO:0000255|HAMAP-Rule:MF_03166, ECO:0000269|PubMed:11812822}.
CC   -!- INDUCTION: Induced in late G1 and early S phase of the cell cycle.
CC       {ECO:0000269|PubMed:17934734, ECO:0000269|PubMed:1938887}.
CC   -!- MISCELLANEOUS: Present with 4820 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03166}.
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DR   EMBL; J04470; AAA35195.1; -; Genomic_DNA.
DR   EMBL; Z46659; CAA86634.1; -; Genomic_DNA.
DR   EMBL; AY693020; AAT93039.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09877.1; -; Genomic_DNA.
DR   PIR; A31425; A31425.
DR   RefSeq; NP_013691.1; NM_001182379.1.
DR   ProteinModelPortal; P12887; -.
DR   SMR; P12887; 99-334.
DR   BioGrid; 35148; 37.
DR   DIP; DIP-8264N; -.
DR   MINT; MINT-4496681; -.
DR   MaxQB; P12887; -.
DR   EnsemblFungi; YML021C; YML021C; YML021C.
DR   GeneID; 854987; -.
DR   KEGG; sce:YML021C; -.
DR   EuPathDB; FungiDB:YML021C; -.
DR   SGD; S000004483; UNG1.
DR   GeneTree; ENSGT00390000003405; -.
DR   HOGENOM; HOG000229528; -.
DR   InParanoid; P12887; -.
DR   KO; K03648; -.
DR   OMA; KCLILGQ; -.
DR   OrthoDB; EOG71ZPC8; -.
DR   BioCyc; YEAST:G3O-32624-MONOMER; -.
DR   Reactome; R-SCE-110329; Cleavage of the damaged pyrimidine.
DR   NextBio; 978118; -.
DR   PRO; PR:P12887; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:SGD.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006281; P:DNA repair; IMP:SGD.
DR   Gene3D; 3.40.470.10; -; 1.
DR   HAMAP; MF_00148; UDG; 1.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR002043; Ura_DNA_glycsylse.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   PANTHER; PTHR11264; PTHR11264; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   TIGRFAMs; TIGR00628; ung; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase;
KW   Mitochondrion; Nucleus; Reference proteome; Transit peptide.
FT   TRANSIT       1     21       Mitochondrion. {ECO:0000255}.
FT   CHAIN        22    359       Uracil-DNA glycosylase.
FT                                /FTId=PRO_0000036085.
FT   ACT_SITE    162    162       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03166}.
FT   CONFLICT    173    173       L -> S (in Ref. 4; AAT93039).
FT                                {ECO:0000305}.
SQ   SEQUENCE   359 AA;  40471 MW;  CC06971E05FE7751 CRC64;
     MWCMRRLPTN SVMTVARKRK QTTIEDFFGT KKSTNEAPNK KGKSGATFMT ITNGAAIKTE
     TKAVAKEANT DKYPANSNAK DVYSKNLSSN LRTLLSLELE TIDDSWFPHL MDEFKKPYFV
     KLKQFVTKEQ ADHTVFPPAK DIYSWTRLTP FNKVKVVIIG QDPYHNFNQA HGLAFSVKPP
     TPAPPSLKNI YKELKQEYPD FVEDNKVGDL THWASQGVLL LNTSLTVRAH NANSHSKHGW
     ETFTKRVVQL LIQDREADGK SLVFLLWGNN AIKLVESLLG STSVGSGSKY PNIMVMKSVH
     PSPLSASRGF FGTNHFKMIN DWLYNTRGEK MIDWSVVPGT SLREVQEANA RLESESKDP
//
#~~# #~+~~+~# #~~#
#LOG 00:00:00 Activity Log for SLiMSuite V1.5.2: Tue Dec 8 11:13:55 2015
#DIR 00:00:00 Run from directory: /srv/slimsuite/logs/prod
#ARG 00:00:00 Commandline arguments: run ip=129.94.146.29 slimfinder&uniprotid=LIG_PCNA_PIPBox_1&dismask=T&jobid=15120800001
#VIO 00:00:00 Verbosity: -1; Interactivity: -1.
#PROG 00:00:00 SLiMFinder V5.2.2: Short Linear Motif Finder
#CMD 00:00:00 Full SLiMFinder CmdList: proglog=F iucut=0.2 usegopher=T protscores=T megablam=F orthdb=qfo_ref.2013-04.all.fas sourcedate=2014-05-28 walltime=0 runid=15120800001 rest=format uniprotid=LIG_PCNA_PIPBox_1.acc dismask=T jobid=15120800001 resfile=slimfinder.csv savespace=0 targz=F megaslim=seqin basefile=slimfinder
#DB 00:00:00 /srv/slimsuite/data/orthdb/qfo_ref.2013-04/qfo_ref.2013-04.all.fas already formatted. (Force = False).
#DB 00:00:00 /srv/slimsuite/data/orthdb/qfo_ref.2013-04/qfo_ref.2013-04.all.fas already formatted. (Force = False).
#ALPH 00:00:00 Alphabet: A C D E F G H I K L M N P Q R S T V W Y
#WARN 00:00:00 NOTE: cloudfix=F. Be wary of ambiguity over-predictions.
#URL 00:00:06 Extracting 18 AccNum from http://www.uniprot.org/uniprot/: 18 read & extracted; 0 failed; 0 duplicates.
#DAT 00:00:06 Extracting entries from slimfinder.dat: 18 read, 18 extracted.
#SEQ 00:00:06 18 sequences loaded from /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.dat (Format: uniprot).
#FAS 00:00:06 18 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.fas.
#UPC 00:00:06 No UPC file found.
#FAS 00:00:06 18 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.slimdb.
#DICT 00:00:06 Made "short" seqName dictionary: 18 seq; 18 keys.
#DB 00:00:06 /share/apps/blast+/2.2.29/bin/makeblastdb -in "/srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.slimdb" -out "/srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.slimdb" -title "/srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.slimdb" -parse_seqids -dbtype prot
#SYS 00:00:06 /share/apps/blast+/2.2.29/bin/blastp -query /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.slimdb -db /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.slimdb -out /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.self.blast -seg yes -comp_based_stats F -soft_masking true -evalue 1.000000e-04 -num_descriptions 18 -num_alignments 18
#INDEX 00:00:07 Indexed "Search" on "Query": 18 unique; 0 missing entries
#CLUST 00:00:07 9 clusters generated from 18 keys (maxdis=1.00)
#DICT 00:00:07 Made "short" seqName dictionary: 18 seq; 18 keys.
#MST 00:00:07 MST for 18 sequences = 15.196.
#UP 00:00:07 slimfinder: 18 Seq; 8 UPC; 15.196 MST; blaste=1.00e-04, blastcf=F, blastf=T
#MAT 00:00:07 slimfinder GABLAM Distance matrix out to /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.dis.tdt (text format).
#MIN 00:00:07 AmbOcc 0.05 & 8 UP => AmbOcc 2 UPC.
#MIN 00:00:07 MinOcc 0.05 & 8 UP => MinOcc 3 UPC.
#DIS 00:00:07 Disorder score file: /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.iupred.txt
#MASK 00:00:07 CDN1A_HUMAN__P38936 masked 7 ordered regions. (29 X added.)
#MASK 00:00:07 DNLI1_HUMAN__P18858 masked 36 ordered regions. (338 X added.)
#MASK 00:00:07 DNLI1_YEAST__P04819 masked 20 ordered regions. (341 X added.)
#MASK 00:00:07 DNMT1_HUMAN__P26358 masked 44 ordered regions. (573 X added.)
#MASK 00:00:07 DPOD3_HUMAN__Q15054 masked 5 ordered regions. (91 X added.)
#MASK 00:00:07 DPOD3_YEAST__P47110 masked 2 ordered regions. (108 X added.)
#MASK 00:00:07 DPOD3_SCHPO__P30261 masked 9 ordered regions. (105 X added.)
#MASK 00:00:07 ERCC5_HUMAN__P28715 masked 16 ordered regions. (218 X added.)
#MASK 00:00:07 FEN1_HUMAN__P39748 masked 8 ordered regions. (154 X added.)
#MASK 00:00:07 FEN1_YEAST__P26793 masked 10 ordered regions. (166 X added.)
#MASK 00:00:07 MSH3_YEAST__P25336 masked 23 ordered regions. (734 X added.)
#MASK 00:00:07 MSH6_HUMAN__P52701 masked 51 ordered regions. (644 X added.)
#MASK 00:00:07 MSH6_YEAST__Q03834 masked 51 ordered regions. (624 X added.)
#MASK 00:00:07 RAD2_YEAST__P07276 masked 25 ordered regions. (247 X added.)
#MASK 00:00:07 RFC1_YEAST__P38630 masked 27 ordered regions. (322 X added.)
#MASK 00:00:07 RRM3_YEAST__P38766 masked 21 ordered regions. (415 X added.)
#MASK 00:00:07 UNG_HUMAN__P13051 masked 11 ordered regions. (103 X added.)
#MASK 00:00:07 UNG_YEAST__P12887 masked 15 ordered regions. (134 X added.)
#FTMASK 00:00:07 FTMask: EM
#MASK 00:00:07 CDN1A_HUMAN__P38936 masked 0 features. (0 X added.)
#MASK 00:00:07 DNLI1_HUMAN__P18858 masked 0 features. (0 X added.)
#MASK 00:00:07 DNLI1_YEAST__P04819 masked 0 features. (0 X added.)
#MASK 00:00:07 DNMT1_HUMAN__P26358 masked 0 features. (0 X added.)
#MASK 00:00:07 DPOD3_HUMAN__Q15054 masked 0 features. (0 X added.)
#MASK 00:00:07 DPOD3_YEAST__P47110 masked 0 features. (0 X added.)
#MASK 00:00:07 DPOD3_SCHPO__P30261 masked 0 features. (0 X added.)
#MASK 00:00:07 ERCC5_HUMAN__P28715 masked 0 features. (0 X added.)
#MASK 00:00:07 FEN1_HUMAN__P39748 masked 0 features. (0 X added.)
#MASK 00:00:07 FEN1_YEAST__P26793 masked 0 features. (0 X added.)
#MASK 00:00:07 MSH3_YEAST__P25336 masked 0 features. (0 X added.)
#MASK 00:00:07 MSH6_HUMAN__P52701 masked 0 features. (0 X added.)
#MASK 00:00:07 MSH6_YEAST__Q03834 masked 0 features. (0 X added.)
#MASK 00:00:07 RAD2_YEAST__P07276 masked 0 features. (0 X added.)
#MASK 00:00:07 RFC1_YEAST__P38630 masked 0 features. (0 X added.)
#MASK 00:00:07 RRM3_YEAST__P38766 masked 0 features. (0 X added.)
#MASK 00:00:07 UNG_HUMAN__P13051 masked 0 features. (0 X added.)
#MASK 00:00:07 UNG_YEAST__P12887 masked 0 features. (0 X added.)
#MASK 00:00:07 Masked DNLI1_HUMAN__P18858 "low complexity" regions. (17 X added.)
#MASK 00:00:07 Masked DNLI1_YEAST__P04819 "low complexity" regions. (3 X added.)
#MASK 00:00:07 Masked DNMT1_HUMAN__P26358 "low complexity" regions. (11 X added.)
#MASK 00:00:07 Masked DPOD3_HUMAN__Q15054 "low complexity" regions. (10 X added.)
#MASK 00:00:07 Masked ERCC5_HUMAN__P28715 "low complexity" regions. (21 X added.)
#MASK 00:00:07 Masked FEN1_YEAST__P26793 "low complexity" regions. (3 X added.)
#MASK 00:00:07 Masked MSH3_YEAST__P25336 "low complexity" regions. (5 X added.)
#MASK 00:00:07 Masked MSH6_HUMAN__P52701 "low complexity" regions. (15 X added.)
#MASK 00:00:07 Masked MSH6_YEAST__Q03834 "low complexity" regions. (11 X added.)
#MASK 00:00:07 Masked RAD2_YEAST__P07276 "low complexity" regions. (10 X added.)
#MASK 00:00:07 Masked RFC1_YEAST__P38630 "low complexity" regions. (11 X added.)
#MASK 00:00:07 Masked RRM3_YEAST__P38766 "low complexity" regions. (3 X added.)
#MASK 00:00:07 Masked UNG_HUMAN__P13051 "low complexity" regions. (3 X added.)
#MASK 00:00:07 Masked UNG_YEAST__P12887 "low complexity" regions. (3 X added.)
#MASK 00:00:07 MetMask: 18 N-terminal Ms masked
#MASK 00:00:07 Masked DPOD3_HUMAN__Q15054 position-specific AAs. (1 X added.)
#MASK 00:00:07 Masked MSH3_YEAST__P25336 position-specific AAs. (1 X added.)
#MASK 00:00:07 Masked MSH6_YEAST__Q03834 position-specific AAs. (1 X added.)
#MASK 00:00:07 slimfinder: Masking of input sequences complete.
#SPACE 00:00:07 Motif Space, 2 positions: 1,200 motifs
#SPACE 00:00:07 Motif Space, 3 positions: 72,000 motifs
#SPACE 00:00:07 Motif Space, 4 positions: 4,320,000 motifs
#SPACE 00:00:07 Motif Space, 5 positions: 259,200,000 motifs
#DIM 00:00:07 Read dimers from 18 seq: 1,221 dimers
#DIM 00:00:07 Reducing dimers: 1,111 >= 2 of 8 UPC
#SLIM 00:00:07 Selecting 2aa SLiMs: 1,111 >= 2 of 8 UPC
#AMB 00:00:07 Adding Wildcard ambiguity: 100.0% (0 amb motifs)
#AMB 00:00:07 Adding Degeneracy ambiguity: 100.0% (0 amb motifs)
#SLIM 00:00:31 Extending 3aa SLiMs >= 2 of 8 UPC: 12,854 SLiMs
#AMB 00:00:35 Adding Wildcard ambiguity: 100.0% (6,028 amb motifs)
#AMB 00:00:46 Adding Degeneracy ambiguity: 100.0% (8,966 amb motifs)
#SLIM 00:01:50 Extending 4aa SLiMs >= 2 of 8 UPC: 8,495 SLiMs
#AMB 00:01:53 Adding Wildcard ambiguity: 100.0% (1,884 amb motifs)
#AMB 00:01:57 Adding Degeneracy ambiguity: 100.0% (1,729 amb motifs)
#SLIM 00:02:33 Extending 5aa SLiMs >= 2 of 8 UPC: 2,158 SLiMs
#AMB 00:02:34 Adding Wildcard ambiguity: 100.0% (58 amb motifs)
#AMB 00:02:39 Adding Degeneracy ambiguity: 100.0% (21 amb motifs)
#SLIM 00:02:39 43,304 SLiMs >= 2 of 8 UPC
#SAVE 00:02:43 SLiMFinder Intermediate saved as /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.l5w2o2a3.FreqDisComp-5-8FT.pickle (Python pickle).
#GZIP 00:02:44 /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.l5w2o2a3.FreqDisComp-5-8FT.pickle zipped.
#SLIM 00:02:44 Filtering 43,304 SLiMs: 23,140 retained.
#PROB 00:02:51 Calculating [Sig] SLiM Probabilities (Sig<=0.10) complete: 50 ranked SLiMs.
#COMB 00:02:52 Combined Occurrence Attributes complete.
#CLOUD 00:02:53 Making "Motif Clouds" for 50 Sig Motifs: 1 Clouds
#SLIM 00:02:54 Cloud 1 (Q..[IL].SFF|Q.[ST]..SFF|Q.[ST][IL]..FF|Q.TL..FF|Q..L..FF|[ST][IL].SFF|TL.SFF|Q.[ST][IL].S.F|Q.[ST][IL].SF|Q..[IL]..FF|Q..I..FF..K|Q.T..SFF|[IL].SFF|TL.{0,1}S.{0,1}FF|Q..L.SFF|Q..I..FF.{1,2}K|TL..FF|Q..[IL].S.F|Q..[IL].SF|K..Q..[IL]..FF|[ST]..SFF|[KR]Q..L..FF|Q.TL..F|Q.TL.S.F|T..SFF|Q.TL.SF|[ST][IL]..FF|Q..I..FF|Q.[ST]..S.F|[KR]..TL..FF|Q.[ST]..SF|L.SFF|Q.T..S.F|I..FF.{1,2}K|Q.[ST][IL]..F|[KR]Q.TL..F|[ILM]..F[FY]|[IL]..FF|TL.S.F|TL.SF|I..FF..K|Q.SI..FF|Q.T..S.{0,1}F|L..FF|[ILMV]..F[FY]|I..FF|KQ..L..FF|Q..L..F|Q.T.{1,2}S.{0,1}FF|Q.T.{1,2}S.F) SLiMMaker: [RST][ILM]..F[FY]
#FREQ 00:02:54 SLiMMaker SLiM matches 17 of 23 sequences (73.9%).
#RANK 00:02:54 Rank calculations complete
#CLOUD 00:02:54 Motif cloud data output to /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.l5w2o2a3.15120800001.cloud.txt for 1 clouds.
#FAS 00:02:54 18 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.l5w2o2a3.15120800001.masked.fas.
#FAS 00:02:55 54 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.l5w2o2a3.15120800001.mapping.fas.
#ALN 00:02:55 Constructing motif alignments: 50 motifs & 18 seqs.: 100.0%.
#FAS 00:02:55 27 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.l5w2o2a3.15120800001.motifaln.fas.
#ALN 00:02:56 Constructing motif alignments: 50 motifs & 18 seqs.: 100.0%.
#FAS 00:02:56 27 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.l5w2o2a3.15120800001.maskaln.fas.
#OCC 00:02:56 Occurrence data output for 357 motif occurrences.
#RES 00:02:56 SLiMFinder results output to /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.csv and /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.occ.csv.
#RES 00:02:56 Additional dataset results output to /srv/slimsuite/scratch/prod/slimfinder/15120800001/slimfinder.*
#END 00:02:56 SLiMFinder server run ended (Finished!): see log file for details.
#WARN 00:02:56 1 warning messages: check log for details.
#LOG 00:02:56 SLiMFinder V5.2.2 End: Tue Dec 8 11:16:51 2015
#JOBID 00:02:56 15120800001
#REST 00:02:56 URL for future retrieval: http://rest.slimsuite.unsw.edu.au/retrieve&jobid=15120800001&rest=format&password=None
#WARN	00:00:00	NOTE: cloudfix=F. Be wary of ambiguity over-predictions.

© 2015 RJ Edwards. Contact: richard.edwards@unsw.edu.au.