ID   MSH3_MAGO7              Reviewed;        1151 AA.
AC   A4R0R0; G4MQQ7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=DNA mismatch repair protein MSH3;
DE   AltName: Full=MutS protein homolog 3;
GN   Name=MSH3; ORFNames=MGG_09306;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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; CM001231; EHA57344.1; -; Genomic_DNA.
DR   RefSeq; XP_003709956.1; XM_003709908.1.
DR   AlphaFoldDB; A4R0R0; -.
DR   SMR; A4R0R0; -.
DR   STRING; 318829.MGG_09306T0; -.
DR   EnsemblFungi; MGG_09306T0; MGG_09306T0; MGG_09306.
DR   GeneID; 2680221; -.
DR   KEGG; mgr:MGG_09306; -.
DR   VEuPathDB; FungiDB:MGG_09306; -.
DR   eggNOG; KOG0218; Eukaryota.
DR   HOGENOM; CLU_002472_0_0_1; -.
DR   InParanoid; A4R0R0; -.
DR   OMA; LRNVHMK; -.
DR   OrthoDB; 138168at2759; -.
DR   Proteomes; UP000009058; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035861; C:site of double-strand break; 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:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0007534; P:gene conversion at mating-type locus; IEA:EnsemblFungi.
DR   GO; GO:0043570; P:maintenance of DNA repeat elements; IEA:EnsemblFungi.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IEA:EnsemblFungi.
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; 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; 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..1151
FT                   /note="DNA mismatch repair protein MSH3"
FT                   /id="PRO_0000338524"
FT   REGION          1..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..347
FT                   /note="Mispair-binding domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        34..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..105
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         913..920
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1151 AA;  126189 MW;  D9B6C63D747E2819 CRC64;
     MAGPSGAAPK KQASLLGFFT PKTVNGLKRP TSSRPGTSEE DEERTADSSP SSRDNVRKRP
     LEQDPDAGNT RRPRASKRAK NVVIDDEDDE HDNDDDDDDF KLDAEAEADP EPVVAADDTA
     GVSQSSSISA SRAGRYIYDE SQPKGQAKTD ENGDALDAAT LRKKRELHDK FVKKLGHPDA
     MSRWGNAGRG EQETGAQEEE EDGDAAEEEP PPPPKGKKKG AKSGKLTPME LQFLEIKRKH
     MDTVLIVEVG YKFRFFGEDA RIAGKELSIV CIPGKFRYDE HPSEAHLDRF ASASIPVHRL
     PVHAKRLVAA GHKVGVVRQI ETAALKKAGD NRNAPFVRKL CEVYTKGTYI DEMGEMDAQT
     GASGAHSGGY LLCLTETAAK GSGTDEKVDV GLVAVQPATG DIIYDSFEDG FMRSEIETRL
     LHISPCELLI VGQLSKATEK LVKHLSGSAS NVFGDRTRVE RVAKGKTTPA EASSHVTKFY
     AGKLKGSTQD DRAAALLDKV LNLPEPVTLC LSAMITHLTE FGLEHIFDLT KYFQSFSTRS
     HMCINGTTLE SLEVYRNSTD HTEKGSLLWA LDKTRTRFGQ RMLRKWLGRP LLDKERLDDR
     VAAVEELFEN RNGPQVEKLQ KLLSSIKTDL ERSLIRIFYG RCTRPELLAV LQTLQRIAVE
     YIVVKEPSQT GFKSNLVSEA LASLPRIREI VVSYLNRINP DAARKNDKYE FFRDESDDTG
     DDGEDEITTQ KMSIAAVEQE LDAHRSDAAA TLGRKKAVDY VTVAGIEYLI EVPNTEIRKV
     PASWAKISGT KKLSRFHTPE VVRLIAERDQ HKEALAAACD AAFKAMLASI ADQYQPLRDA
     VSSLATLDCL LSFAQVAALP GYSKPIILPD SHPPTIAVAG GRHPIAEHTL PSGYIPFSTT
     LSSPAPLAHL VTGPNMGGKS SFVRALALLV LLAQVGSFVP ADSLRLTLSD AIYTRMGASD
     NLFAGESTFM VEVGETAAIL RTATPRSLVL LDELGRGTST HDGAAIAHAV LDHVVRNTRC
     LTLFITHYQS LARVAEGLGT GLVRNVHMRF TSSRDDNDDG DKDQDDDVGE NITFLYEVAD
     GVAHRSYGLN VARLARIPRK ILEVAARKSR KMEEDVRTRR LRSATKLLEA VCRGDGSDDQ
     LEHLLSSIEQ L