ID   MSH3_VANPO              Reviewed;        1023 AA.
AC   A7TTQ1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=DNA mismatch repair protein MSH3;
DE   AltName: Full=MutS protein homolog 3;
GN   Name=MSH3; ORFNames=Kpol_183p2;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480605; EDO14357.1; -; Genomic_DNA.
DR   RefSeq; XP_001642215.1; XM_001642165.1.
DR   AlphaFoldDB; A7TTQ1; -.
DR   SMR; A7TTQ1; -.
DR   STRING; 436907.A7TTQ1; -.
DR   EnsemblFungi; EDO14357; EDO14357; Kpol_183p2.
DR   GeneID; 5542335; -.
DR   KEGG; vpo:Kpol_183p2; -.
DR   eggNOG; KOG0218; Eukaryota.
DR   HOGENOM; CLU_002472_0_0_1; -.
DR   InParanoid; A7TTQ1; -.
DR   OMA; LRNVHMK; -.
DR   OrthoDB; 138168at2759; -.
DR   PhylomeDB; A7TTQ1; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
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; 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; 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; 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; 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..1023
FT                   /note="DNA mismatch repair protein MSH3"
FT                   /id="PRO_0000338532"
FT   REGION          19..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..259
FT                   /note="Mispair-binding domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        19..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         792..799
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1023 AA;  117059 MW;  2A1A7FF99F8FA1D4 CRC64;
     MSKQPVISRF FKPIARKEVT SEKGVEKEKP VDLDEEKHNE PATTSRLMPK GFDAAAETVT
     DEVIEIEVEI EHESEPKIEI KNGTVTAENK SMDFAEKLNR IWNDKKRVIS NNDNDDSDGE
     NDTIVKKSKN NSNKLTPLDQ QVKDLKLLHM DKILVIRVGY KYKCFAQDAE IVSKILHIML
     IPGKLTIDES NPQDSNYRQF AYCSFPDIRL KVHLETLVHN NLKVAVVEQS ETSAIKKNSN
     ASSKNSVFER KISGVYTKAT FGINSAFSSN RKNVLGQYNS IWIINFSEID KINSSFFMIS
     VNLNSGEIIY DTFECSTTSI ENLETRIKYL NPIEVLTVSA LPEKVKLRLH GSNSTILLKE
     KEDIDKEIME EINKSTKGLN LSAELFELVP VLYKYLTEYN NEELLLISEN YKPFASKKHM
     VLNAAAIESL GIFGEEGGKG SLFWLLDHTR TSFGSRKLRE WILHPLLDKK EIEDRLDAVD
     CIIHEVSNIF FESLNKMLTN VPDLLRTINR IAYGTTSRKE IYYFLKQMKS FSDHFQLHSN
     YLNSQVVSND GRIHKSSALL TNLLTEITSG LKEINIENIL SMINVSSVME KDTYKQVSEF
     FNLNYYDHAE EIIKIQGNIN EVKNELAEEL SSIRKILKRP HLNYKDEMDY LIEVRNTQTK
     GLPSDWIVVN RTKMISRYHT PTSRKLIEKL QYQKDILYQE TQKEYFQFVK RIKNDYFALN
     KIINHIATYD CILALASTSQ NMNYVRPVLT DESQFIDAKN ARNPIIESLD INYVPNDVNL
     SHSAGKFLII TGPNMGGKSS YIRQVALLVI LAQVGSYVPA DFMKTSIFDK ILTRIGAYDN
     LLKGQSTFKV ELLEIQNIIK NKTENSLLLL DEVGRGTSTE DGKAISYSIV DYFINLPVCP
     LVLFTTHYPF LGSINSKILK SYYMDFVEQK KEGEDWPSIV FLYKLRSGIT DSSFGLNVAR
     LAQIDKDIIN HAFSISEKIR QETETANTMN LPILLKHILS SNDLKPQQKI IEILNLQNDS
     QEL