MSH3_CANGA
ID MSH3_CANGA Reviewed; 1025 AA.
AC Q6FVN6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; OrderedLocusNames=CAGL0E00473g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Heterodimerizes with MSH2 to form MutS beta, which binds to DNA
CC mismatches thereby initiating DNA repair. MSH3 provides substrate-
CC binding and substrate specificity to the complex. When bound, the MutS
CC beta heterodimer bends the DNA helix and shields approximately 20 base
CC pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to
CC 13 nucleotides in size, but can also repair base-base and single
CC insertion-deletion mismatches that occur during replication. After
CC mismatch binding, forms a ternary complex with the MutL alpha
CC heterodimer, which is thought to be responsible for directing the
CC downstream MMR events, including strand discrimination, excision, and
CC resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch
CC repair functions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC ternary complex with MutL alpha (MLH1-PMS1) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000305}.
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DR EMBL; CR380951; CAG58627.1; -; Genomic_DNA.
DR RefSeq; XP_445708.1; XM_445708.1.
DR AlphaFoldDB; Q6FVN6; -.
DR SMR; Q6FVN6; -.
DR STRING; 5478.XP_445708.1; -.
DR EnsemblFungi; CAG58627; CAG58627; CAGL0E00473g.
DR GeneID; 2887527; -.
DR KEGG; cgr:CAGL0E00473g; -.
DR CGD; CAL0128716; CAGL0E00473g.
DR VEuPathDB; FungiDB:CAGL0E00473g; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_0_1; -.
DR InParanoid; Q6FVN6; -.
DR OMA; LRNVHMK; -.
DR Proteomes; UP000002428; Chromosome E.
DR GO; GO:0032302; C:MutSbeta complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000406; F:double-strand/single-strand DNA junction binding; IEA:EnsemblFungi.
DR GO; GO:0000404; F:heteroduplex DNA loop binding; IEA:EnsemblFungi.
DR GO; GO:0000403; F:Y-form DNA binding; IEA:EnsemblFungi.
DR GO; GO:0000710; P:meiotic mismatch repair; IEA:EnsemblFungi.
DR GO; GO:0006312; P:mitotic recombination; IEA:EnsemblFungi.
DR GO; GO:0000735; P:removal of nonhomologous ends; IEA:EnsemblFungi.
DR GO; GO:0043111; P:replication fork arrest; IEA:EnsemblFungi.
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; IPR017261; DNA_mismatch_repair_MutS/MSH.
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; IPR036187; DNA_mismatch_repair_MutS_sf.
DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361; PTHR11361; 1.
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 PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 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 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..1025
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000338516"
FT REGION 41..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..272
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 131..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 800..807
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1025 AA; 117474 MW; FDB77ADEC95A0900 CRC64;
MKQASISRFF KKVSAVNKEK VDQVKEVEKE AEVDEVLDLT LDSENDEEQQ QETPVLEPID
GEEHPTVSKV PDLNDSRLLQ KQKILNASKD ITNSVDVSAF NEKLKDIMNK RKLGRIKGSL
IDESDEIAEQ SEADEHNIKK KRKKSDQLTP LDRQVKDLKL GNMDKVLVIR VGYKYKIFAQ
DAIIASTILH LQLIPGKVTI DDSNPNDSKY KQFAYCSFPD VRLKVHLERL VRSGLKVAVV
EQSETATTKK FDNSKAKTSV FERKITGTYS KATYATNCEF EVNHENILGT NNSIWALDIE
VSDSIYKYYL WSIQLSNGEV IYDSFEESKD NFSKVETRMK YLNPSEIVSP VVDSFPIKLK
KRFLDLQLCQ KNYDILAEDL NIPKKELLNN RLIELWHILY RYLKEYSNEK LLNIGSNYRH
FSQKISIQLQ AQTINNLDLI SNDDSKGTLF WILDHTRTPF GKRLLKEWLL RPLLSKDAIV
DRLNAIDCIL ESANSIFFES LNQMMKGIPD LLRTINRVSF GKTSQREVYF LLKQLTGVIK
HFEAHKDYIE VEINSNSGAI KTKSTKLASI MTQMFEFSLS SVIPQLLLMI NVSAVMEKDQ
KKQLLGFFHL NNYDNSENII KMQRDIDSVK AQLHDELQNI KKILKRPHLA YKDEVDFLIE
VRNTQVKGIP SDWVKVNNTK MISRFLTPRT KELVELLEYQ NDLLYNEISK EYDQFLNRIA
SYYNEVKTFI MNLAEYDCLL SLAAVSCNVG YTRPVFTDSN EQLIIAKQAR NPIIESLGVD
YVPNDIEMEK DSGRVLVITG PNMGGKSSYI RQIALMVIMA QIGSYVPAES LKLSVFDNVL
TRIGSQDNIL QGQSTFKVEL SETVEIINSC TSKTLLLLDE VGRGTSTRDG NAIAWALIKY
FVEEEQCPFI LFTTHFTIVT TVKSPLLKSY HMNYVQHKNE NENWTTVVFL YQLKAGVTDS
SYGLNVAKLA GIDTHIINRA HDVAISYKND TEFDTNMILF QKVRNILANR TTARETLKVL
LELDV
