PMS1_YEAST
ID PMS1_YEAST Reviewed; 873 AA.
AC P14242; D6W197; Q2I044; Q2I045; Q45TY4; Q8TG48; Q8TG50; Q8TG54; Q8TG57;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=DNA mismatch repair protein PMS1;
DE AltName: Full=Postmeiotic segregation protein 1;
GN Name=PMS1; OrderedLocusNames=YNL082W; ORFNames=N2317;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2676974; DOI=10.1128/jb.171.10.5339-5346.1989;
RA Kramer W., Kramer B., Williamson M.S., Fogel S.;
RT "Cloning and nucleotide sequence of DNA mismatch repair gene PMS1 from
RT Saccharomyces cerevisiae: homology of PMS1 to procaryotic MutL and HexB.";
RL J. Bacteriol. 171:5339-5346(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-41; THR-112; VAL-384;
RP VAL-392; SER-400; SER-401; 416-THR--THR-420; ASN-475; VAL-564; ARG-768 AND
RP LYS-818.
RC STRAIN=ATCC 200060 / W303, S96, SK1, YJM 339, and YJM 421;
RX PubMed=11907579; DOI=10.1038/416326a;
RA Steinmetz L.M., Sinha H., Richards D.R., Spiegelman J.I., Oefner P.J.,
RA McCusker J.H., Davis R.W.;
RT "Dissecting the architecture of a quantitative trait locus in yeast.";
RL Nature 416:326-330(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-41; THR-112; VAL-384;
RP SER-400; 416-THR--THR-420; PHE-513 AND LYS-818.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-458.
RC STRAIN=EAY1066, EAY1068, M2-8, M5-7, and M7-8;
RX PubMed=16492773; DOI=10.1073/pnas.0510998103;
RA Heck J.A., Argueso J.L., Gemici Z., Reeves R.G., Bernard A., Aquadro C.F.,
RA Alani E.;
RT "Negative epistasis between natural variants of the Saccharomyces
RT cerevisiae MLH1 and PMS1 genes results in a defect in mismatch repair.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3256-3261(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701611;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<391::aid-yea921>3.0.co;2-n;
RA Poehlmann R., Philippsen P.;
RT "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV
RT reveals 12 new open reading frames (ORFs) and an ancient duplication of six
RT ORFs.";
RL Yeast 12:391-402(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [7]
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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-225.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740422;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<485::aid-yea928>3.0.co;2-u;
RA Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A.;
RT "The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome
RT XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading
RT frames.";
RL Yeast 12:485-491(1996).
RN [9]
RP INTERACTION WITH MLH1, AND MUTAGENESIS OF PHE-95.
RX PubMed=9234704; DOI=10.1128/mcb.17.8.4465;
RA Pang Q., Prolla T.A., Liskay R.M.;
RT "Functional domains of the Saccharomyces cerevisiae Mlh1p and Pms1p DNA
RT mismatch repair proteins and their relevance to human hereditary
RT nonpolyposis colorectal cancer-associated mutations.";
RL Mol. Cell. Biol. 17:4465-4473(1997).
RN [10]
RP FUNCTION, AND SUBUNIT.
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 mismatch
RT and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes.";
RL J. Biol. Chem. 273:9837-9841(1998).
RN [11]
RP FUNCTION, AND INTERACTION WITH MLH1.
RX PubMed=10570173; DOI=10.1073/pnas.96.24.13914;
RA Wang T.-F., Kleckner N., Hunter N.;
RT "Functional specificity of MutL homologs in yeast: evidence for three Mlh1-
RT based heterocomplexes with distinct roles during meiosis in recombination
RT and mismatch correction.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13914-13919(1999).
RN [12]
RP INTERACTION WITH MLH1, ATP-BINDING, AND MUTAGENESIS OF GLU-30 AND GLY-97.
RX PubMed=10938116; DOI=10.1128/mcb.20.17.6390-6398.2000;
RA Tran P.T., Liskay R.M.;
RT "Functional studies on the candidate ATPase domains of Saccharomyces
RT cerevisiae MutLalpha.";
RL Mol. Cell. Biol. 20:6390-6398(2000).
RN [13]
RP DNA-BINDING.
RX PubMed=12222686; DOI=10.1515/bc.2002.103;
RA Drotschmann K., Hall M.C., Shcherbakova P.V., Wang H., Erie D.A.,
RA Brownewell F.R., Kool E.T., Kunkel T.A.;
RT "DNA binding properties of the yeast Msh2-Msh6 and Mlh1-Pms1
RT heterodimers.";
RL Biol. Chem. 383:969-975(2002).
RN [14]
RP ATP-BINDING, MUTAGENESIS OF GLU-30 AND ASN-34, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=11717305; DOI=10.1074/jbc.m106120200;
RA Hall M.C., Shcherbakova P.V., Kunkel T.A.;
RT "Differential ATP binding and intrinsic ATP hydrolysis by amino-terminal
RT domains of the yeast Mlh1 and Pms1 proteins.";
RL J. Biol. Chem. 277:3673-3679(2002).
RN [15]
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 [16]
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 [17]
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., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [18]
RP DNA-BINDING, AND MUTAGENESIS OF LYS-297.
RX PubMed=12682353; DOI=10.1093/nar/gkg324;
RA Hall M.C., Shcherbakova P.V., Fortune J.M., Borchers C.H., Dial J.M.,
RA Tomer K.B., Kunkel T.A.;
RT "DNA binding by yeast Mlh1 and Pms1: implications for DNA mismatch
RT repair.";
RL Nucleic Acids Res. 31:2025-2034(2003).
RN [19]
RP FUNCTION, AND MUTAGENESIS OF GLY-851 AND HIS-857.
RX PubMed=16227575; DOI=10.1128/mcb.25.21.9221-9231.2005;
RA Erdeniz N., Dudley S., Gealy R., Jinks-Robertson S., Liskay R.M.;
RT "Novel PMS1 alleles preferentially affect the repair of primer strand loops
RT during DNA replication.";
RL Mol. Cell. Biol. 25:9221-9231(2005).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION BY
RP 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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, AND IDENTIFICATION BY
RP 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 insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Required for DNA mismatch repair (MMR), correcting base-base
CC mismatches and insertion-deletion loops (IDLs) resulting from DNA
CC replication, DNA damage or from recombination events between non-
CC identical sequences during meiosis. Component of the MutLalpha
CC heterodimer that forms a ternary complex with the MutS heterodimers,
CC which initially recognize the DNA mismatches. This complex is thought
CC to be responsible for directing the downsteam MMR events, including
CC strand discrimination, excision, and resynthesis. Plays a major role in
CC maintaining the genetic stability of simple sequence repeats and in the
CC repair of heteroduplex sites present in meiotic recombination
CC intermediates. {ECO:0000269|PubMed:10570173,
CC ECO:0000269|PubMed:16227575, ECO:0000269|PubMed:9545323}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for ATP {ECO:0000269|PubMed:11717305};
CC -!- SUBUNIT: Heterodimer of MLH1 and PMS1, called MutLalpha, which is the
CC major MMR MutL activity correcting base-base mismatches as well as
CC IDLs. The heterodimer binds double strand DNA independently of a
CC mismatch with positive cooperativity and has more than one DNA binding
CC site. Forms a ternary complex with either the MSH2-MSH6 (MutSalpha) or
CC the MSH2-MSH3 heterodimer (MutSbeta), which recognize and bind to
CC mismatch DNA. Ternary complex formation is promoted by ATP binding.
CC {ECO:0000269|PubMed:9545323}.
CC -!- INTERACTION:
CC P14242; P38920: MLH1; NbExp=12; IntAct=EBI-13561, EBI-11003;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34885.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAM00521.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAM00533.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAM00545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAM00551.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAM00563.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAM00569.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA60176.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA61428.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA95956.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA95957.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M29688; AAA34885.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF458969; AAM00521.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF458971; AAM00533.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF458973; AAM00545.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF458974; AAM00551.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF458976; AAM00563.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF458977; AAM00569.1; ALT_INIT; Genomic_DNA.
DR EMBL; DQ115393; AAZ22526.1; -; Genomic_DNA.
DR EMBL; DQ356628; ABC86932.1; -; Genomic_DNA.
DR EMBL; DQ356629; ABC86933.1; -; Genomic_DNA.
DR EMBL; DQ356630; ABC86934.1; -; Genomic_DNA.
DR EMBL; DQ356631; ABC86935.1; -; Genomic_DNA.
DR EMBL; DQ356632; ABC86936.1; -; Genomic_DNA.
DR EMBL; X86470; CAA60176.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z71357; CAA95956.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z71358; CAA95957.1; ALT_INIT; Genomic_DNA.
DR EMBL; X89016; CAA61428.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006947; DAA10463.1; -; Genomic_DNA.
DR PIR; S53896; S53896.
DR RefSeq; NP_014317.4; NM_001182920.3.
DR PDB; 3H4L; X-ray; 2.50 A; A/B=1-365.
DR PDB; 4E4W; X-ray; 2.50 A; B=635-873.
DR PDB; 4FMN; X-ray; 2.69 A; B=635-873.
DR PDB; 4FMO; X-ray; 3.04 A; B=635-873.
DR PDBsum; 3H4L; -.
DR PDBsum; 4E4W; -.
DR PDBsum; 4FMN; -.
DR PDBsum; 4FMO; -.
DR AlphaFoldDB; P14242; -.
DR SMR; P14242; -.
DR BioGRID; 35741; 244.
DR ComplexPortal; CPX-1666; MutLalpha endonuclease complex.
DR DIP; DIP-2416N; -.
DR IntAct; P14242; 8.
DR MINT; P14242; -.
DR STRING; 4932.YNL082W; -.
DR iPTMnet; P14242; -.
DR MaxQB; P14242; -.
DR PaxDb; P14242; -.
DR PRIDE; P14242; -.
DR EnsemblFungi; YNL082W_mRNA; YNL082W; YNL082W.
DR GeneID; 855642; -.
DR KEGG; sce:YNL082W; -.
DR SGD; S000005026; PMS1.
DR VEuPathDB; FungiDB:YNL082W; -.
DR eggNOG; KOG1978; Eukaryota.
DR GeneTree; ENSGT00940000155381; -.
DR HOGENOM; CLU_004131_0_2_1; -.
DR InParanoid; P14242; -.
DR OMA; SFNNVQY; -.
DR BioCyc; YEAST:G3O-33111-MON; -.
DR Reactome; R-SCE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR EvolutionaryTrace; P14242; -.
DR PRO; PR:P14242; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P14242; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0032300; C:mismatch repair complex; IBA:GO_Central.
DR GO; GO:0032389; C:MutLalpha complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IMP:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0000710; P:meiotic mismatch repair; IDA:ComplexPortal.
DR GO; GO:0006298; P:mismatch repair; IMP:SGD.
DR Gene3D; 3.30.1370.100; -; 1.
DR Gene3D; 3.30.1540.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR014762; DNA_mismatch_repair_CS.
DR InterPro; IPR002099; DNA_mismatch_repair_N.
DR InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR038973; MutL/Mlh/Pms.
DR InterPro; IPR014790; MutL_C.
DR InterPro; IPR042120; MutL_C_dimsub.
DR InterPro; IPR042121; MutL_C_regsub.
DR InterPro; IPR037198; MutL_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10073; PTHR10073; 1.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR Pfam; PF08676; MutL_C; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SMART; SM00853; MutL_C; 1.
DR SUPFAM; SSF118116; SSF118116; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00585; mutl; 1.
DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..873
FT /note="DNA mismatch repair protein PMS1"
FT /id="PRO_0000245571"
FT REGION 1..357
FT /note="DNA- and ATP-binding"
FT REGION 379..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..873
FT /note="Interaction with MLH1"
FT COMPBIAS 379..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 41
FT /note="N -> S (in strain: SK1 and YJM421)"
FT /evidence="ECO:0000269|PubMed:11907579,
FT ECO:0000269|PubMed:16273108"
FT VARIANT 112
FT /note="I -> T (in strain: SK1 and YJM421)"
FT /evidence="ECO:0000269|PubMed:11907579,
FT ECO:0000269|PubMed:16273108"
FT VARIANT 384
FT /note="F -> V (in strain: SK1, YJM320, YJM339 and YJM421)"
FT /evidence="ECO:0000269|PubMed:11907579,
FT ECO:0000269|PubMed:16273108"
FT VARIANT 392
FT /note="E -> V (in strain: YJM320)"
FT /evidence="ECO:0000269|PubMed:11907579"
FT VARIANT 400
FT /note="T -> S (in strain: SK1, YJM320, YJM339 and YJM421)"
FT /evidence="ECO:0000269|PubMed:11907579,
FT ECO:0000269|PubMed:16273108"
FT VARIANT 401
FT /note="A -> S (in strain: YJM320 and YJM421)"
FT /evidence="ECO:0000269|PubMed:11907579"
FT VARIANT 416
FT /note="T -> TCEGT (in strain: SK1, YJM320, YJM339 and
FT YJM421)"
FT VARIANT 458
FT /note="D -> Y (in strain: EAY1068)"
FT /evidence="ECO:0000269|PubMed:16492773"
FT VARIANT 475
FT /note="D -> N (in strain: YJM339)"
FT /evidence="ECO:0000269|PubMed:11907579"
FT VARIANT 513
FT /note="Y -> F (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 564
FT /note="A -> V (in strain: YJM320)"
FT /evidence="ECO:0000269|PubMed:11907579"
FT VARIANT 768
FT /note="K -> R (in strain: YJM320)"
FT /evidence="ECO:0000269|PubMed:11907579"
FT VARIANT 818
FT /note="R -> K (in strain: SK1 and YJM320; forms a non-
FT functional heterodimer with MHL1 from strain S288c,
FT resulting in an accumulation of mutations in spore progeny
FT of crosses between these strains)"
FT /evidence="ECO:0000269|PubMed:11907579,
FT ECO:0000269|PubMed:16273108"
FT MUTAGEN 30
FT /note="E->A: Reduces ATPase activity by 62%. Displays 60-
FT fold increase in spontaneous mutation accumulation."
FT /evidence="ECO:0000269|PubMed:10938116,
FT ECO:0000269|PubMed:11717305"
FT MUTAGEN 34
FT /note="N->A: Reduces ATPase activity by 84%. Displays
FT 11000-fold increase in spontaneous mutation accumulation."
FT /evidence="ECO:0000269|PubMed:11717305"
FT MUTAGEN 95
FT /note="F->A: Displays an increase in spontaneous mutation
FT accumulation. Does not impair heterodimer formation."
FT /evidence="ECO:0000269|PubMed:9234704"
FT MUTAGEN 97
FT /note="G->A: Displays an increase in spontaneous mutation
FT accumulation."
FT /evidence="ECO:0000269|PubMed:10938116"
FT MUTAGEN 297
FT /note="K->E: Displays a 60-fold increase in spontaneous
FT mutation accumulation."
FT /evidence="ECO:0000269|PubMed:12682353"
FT MUTAGEN 851
FT /note="G->E: Confers a strong defect in the repair of
FT primer strand-specific 1-bp loops during DNA replication,
FT but not during meoitic recombination. Does not impair
FT heterodimer formation."
FT /evidence="ECO:0000269|PubMed:16227575"
FT MUTAGEN 857
FT /note="H->R: Confers a strong defect in the repair of
FT primer strand-specific 1-bp loops during DNA replication,
FT but not during meoitic recombination. Does not impair
FT heterodimer formation."
FT /evidence="ECO:0000269|PubMed:16227575"
FT CONFLICT 695
FT /note="Y -> S (in Ref. 1; AAA34885)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="L -> I (in Ref. 1; AAA34885)"
FT /evidence="ECO:0000305"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:3H4L"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:3H4L"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:3H4L"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3H4L"
FT TURN 69..73
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:3H4L"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 140..149
FT /evidence="ECO:0007829|PDB:3H4L"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:3H4L"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:3H4L"
FT HELIX 165..182
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3H4L"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:3H4L"
FT TURN 221..226
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:3H4L"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 274..285
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:3H4L"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:3H4L"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:3H4L"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:3H4L"
FT HELIX 341..361
FT /evidence="ECO:0007829|PDB:3H4L"
FT HELIX 650..652
FT /evidence="ECO:0007829|PDB:4E4W"
FT HELIX 653..665
FT /evidence="ECO:0007829|PDB:4E4W"
FT HELIX 668..672
FT /evidence="ECO:0007829|PDB:4E4W"
FT STRAND 675..680
FT /evidence="ECO:0007829|PDB:4E4W"
FT TURN 681..683
FT /evidence="ECO:0007829|PDB:4E4W"
FT STRAND 684..690
FT /evidence="ECO:0007829|PDB:4E4W"
FT STRAND 695..701
FT /evidence="ECO:0007829|PDB:4E4W"
FT HELIX 702..717
FT /evidence="ECO:0007829|PDB:4E4W"
FT STRAND 722..731
FT /evidence="ECO:0007829|PDB:4E4W"
FT HELIX 739..742
FT /evidence="ECO:0007829|PDB:4E4W"
FT HELIX 747..750
FT /evidence="ECO:0007829|PDB:4E4W"
FT STRAND 767..773
FT /evidence="ECO:0007829|PDB:4E4W"
FT HELIX 782..794
FT /evidence="ECO:0007829|PDB:4E4W"
FT HELIX 806..819
FT /evidence="ECO:0007829|PDB:4E4W"
FT HELIX 829..838
FT /evidence="ECO:0007829|PDB:4E4W"
FT HELIX 839..841
FT /evidence="ECO:0007829|PDB:4E4W"
FT STRAND 842..844
FT /evidence="ECO:0007829|PDB:4E4W"
FT STRAND 853..860
FT /evidence="ECO:0007829|PDB:4E4W"
FT HELIX 869..871
FT /evidence="ECO:0007829|PDB:4E4W"
SQ SEQUENCE 873 AA; 99355 MW; 2E0FFBC59B718854 CRC64;
MTQIHQINDI DVHRITSGQV ITDLTTAVKE LVDNSIDANA NQIEIIFKDY GLESIECSDN
GDGIDPSNYE FLALKHYTSK IAKFQDVAKV QTLGFRGEAL SSLCGIAKLS VITTTSPPKA
DKLEYDMVGH ITSKTTTSRN KGTTVLVSQL FHNLPVRQKE FSKTFKRQFT KCLTVIQGYA
IINAAIKFSV WNITPKGKKN LILSTMRNSS MRKNISSVFG AGGMRGLEEV DLVLDLNPFK
NRMLGKYTDD PDFLDLDYKI RVKGYISQNS FGCGRNSKDR QFIYVNKRPV EYSTLLKCCN
EVYKTFNNVQ FPAVFLNLEL PMSLIDVNVT PDKRVILLHN ERAVIDIFKT TLSDYYNRQE
LALPKRMCSQ SEQQAQKRLK TEVFDDRSTT HESDNENYHT ARSESNQSNH AHFNSTTGVI
DKSNGTELTS VMDGNYTNVT DVIGSECEVS VDSSVVLDEG NSSTPTKKLP SIKTDSQNLS
DLNLNNFSNP EFQNITSPDK ARSLEKVVEE PVYFDIDGEK FQEKAVLSQA DGLVFVDNEC
HEHTNDCCHQ ERRGSTDTEQ DDEADSIYAE IEPVEINVRT PLKNSRKSIS KDNYRSLSDG
LTHRKFEDEI LEYNLSTKNF KEISKNGKQM SSIISKRKSE AQENIIKNKD ELEDFEQGEK
YLTLTVSKND FKKMEVVGQF NLGFIIVTRK VDNKYDLFIV DQHASDEKYN FETLQAVTVF
KSQKLIIPQP VELSVIDELV VLDNLPVFEK NGFKLKIDEE EEFGSRVKLL SLPTSKQTLF
DLGDFNELIH LIKEDGGLRR DNIRCSKIRS MFAMRACRSS IMIGKPLNKK TMTRVVHNLS
ELDKPWNCPH GRPTMRHLME LRDWSSFSKD YEI
