MSH3_ASHGO
ID MSH3_ASHGO Reviewed; 1032 AA.
AC Q759V4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; OrderedLocusNames=ADR168C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52089.1; -; Genomic_DNA.
DR RefSeq; NP_984265.1; NM_209618.1.
DR AlphaFoldDB; Q759V4; -.
DR SMR; Q759V4; -.
DR STRING; 33169.AAS52089; -.
DR EnsemblFungi; AAS52089; AAS52089; AGOS_ADR168C.
DR GeneID; 4620427; -.
DR KEGG; ago:AGOS_ADR168C; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_0_1; -.
DR InParanoid; Q759V4; -.
DR OMA; LRNVHMK; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0032302; C:MutSbeta complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0003690; F:double-stranded DNA binding; IBA:GO_Central.
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:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0000735; P:removal of nonhomologous ends; IEA:EnsemblFungi.
DR GO; GO:0043111; P:replication fork arrest; 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; 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; 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..1032
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000338507"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..262
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 796..803
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1032 AA; 117140 MW; FB89500518B0871B CRC64;
MLQQPTISRF FKSSSTRKKS EQRTAKEEAE LMQLLESDGE NNSATVPSDR KPEAAPMHVG
LGNKAAAGGA VPGQVKSATR GFEDFRFNRR REACGKEQEV GFAERLQRIM ERREGGCVEE
DETELDNEAP RSKRAKPNRL TELDQQFKDL KLQHMDKVLA VRVGYKYKFF AEDAVMVSRV
LQIKLVPGKL TVHETDPADH KHKKFAYCTI PDTRLEVHLQ RLMHHNLKVG VVEQTETSAV
KKNSGTSSSV FSREVTNIFT RATYGINETF GTKDRRVLGD SASVWGLVCK RQPSYTRYFL
VSVNLNSGEV IFDDFKEERF LTEALETRIK YTNPSEVVVG DGLGSEIEKV FHTSDSDITL
NRIELVGLYE EIFSEPHPAF KGNVPLQTAL MLVHGYLTNF KNESLLFFKE NFKPFCSKTH
MILPSSAIES LDIFENSTDR SSKGSLLWVL DHTRTNYGLR NLKNWIAKPL INIDQIQQRL
DAVQCISTEV GNIFIESLNN MLRDGQDLER ILNRIAYGKT SRREVYLFLR ELTQLATLFS
SHHRYIETNV LSANGKIRMQ SSLLANIFTD LDEYWKQFPI PNFLAMINID AALDKNPDRP
YVEYFNLTKY DRAEPLISKQ QDIEAVIGEL RDELKNIRVI LKRPMLNYKD EIDFLVEIRN
TQVSSVPVDW VKVASTKAVS RFQTPGTAKL VAKLQYHKEL LQDLALQEYE SFIKRITGEY
TSLRKAILHL STYDCILSLA ATSCNVDYVR PKFNTAPQCI NVINGRNPII ESLDVRYMPN
DVNLNREGKK IMIITGPNMG GKSSYIRQVA LLVIMAQIGC YVPAQEAEFS IFDQIFTRIG
AYDNLLRNDS TFKIEMTEMV QILRSSTENS LLLLDEVGRG TGTHDGISIS YALLRYFIEL
HNACPLILFI THYASLGSIR SPILGNYHMS YIEEKRPGEN WPSVVFLYKL KEGRAHNSYG
LNVAKLADIQ TGIINRAYKI STMLKQEMES NSSIAAICTI KHALAGNSAA SLKSAIETLI
ESADHEQFVL NM
