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Database: UniProt
Entry: A0A1S9DUM3_ASPOZ
LinkDB: A0A1S9DUM3_ASPOZ
Original site: A0A1S9DUM3_ASPOZ 
ID   A0A1S9DUM3_ASPOZ        Unreviewed;       940 AA.
AC   A0A1S9DUM3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=DNA mismatch repair protein MSH3 {ECO:0000256|ARBA:ARBA00019000};
DE   AltName: Full=DNA mismatch repair protein msh3 {ECO:0000256|ARBA:ARBA00022151};
GN   ORFNames=OAory_01003350 {ECO:0000313|EMBL:OOO12586.1};
OS   Aspergillus oryzae (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO12586.1, ECO:0000313|Proteomes:UP000190312};
RN   [1] {ECO:0000313|EMBL:OOO12586.1, ECO:0000313|Proteomes:UP000190312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC7051 {ECO:0000313|EMBL:OOO12586.1,
RC   ECO:0000313|Proteomes:UP000190312};
RA   Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA   Jeennor S., Laoteng K.;
RT   "Genome sequencing of Aspergillus oryzae BCC7051.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025373}.
CC   -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC       ternary complex with MutL alpha (MLH1-PMS1).
CC       {ECO:0000256|ARBA:ARBA00025902}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC       {ECO:0000256|ARBA:ARBA00006271, ECO:0000256|RuleBase:RU003756}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OOO12586.1}.
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DR   EMBL; MKZY01000002; OOO12586.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9DUM3; -.
DR   VEuPathDB; FungiDB:AO090005001261; -.
DR   eggNOG; KOG0219; Eukaryota.
DR   OMA; LVRFPQK; -.
DR   Proteomes; UP000190312; 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   CDD; cd03285; ABC_MSH2_euk; 1.
DR   Gene3D; 1.10.1420.10; -; 2.
DR   Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR   Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR011184; DNA_mismatch_repair_Msh2.
DR   InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
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; IPR032642; Msh2_ATP-bd.
DR   InterPro; IPR036678; MutS_con_dom_sf.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11361:SF35; DNA MISMATCH REPAIR PROTEIN MSH2; 1.
DR   PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 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; PIRSF005813; MSH2; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU003756};
KW   DNA repair {ECO:0000256|RuleBase:RU003756};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003756};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003756}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190312}.
FT   DOMAIN          737..753
FT                   /note="DNA mismatch repair proteins mutS family"
FT                   /evidence="ECO:0000259|PROSITE:PS00486"
SQ   SEQUENCE   940 AA;  105594 MW;  2F4E154F14731F71 CRC64;
     MSSRPELKVD DEVGFIRFYR SLAANSNDET IRVFDRGDWY SAHGAEAEFI ARTVYKTTSI
     LRNLGRSDSG GLPSVTMSVT VFRNFLREAL FRLNKRIEIW GSVGTGKGHW KLVKQASPGN
     LQDVEEELGS VGGLSMDSAP IILAVKISAK AAEARSVGVC FADASVRELG VSEFLDNDIY
     SNFESLIIQL GVKECLVQMD ANKKDVELGK IRAIADSCGI AISERPVADY GVKDIEQDLT
     RLLRDERSAG TLPQTELKLA MGSASALIKY LGVMTDPTNF GQYQLYQHDL SQFMKLDSSA
     LRALNLMPGP RDGSKSMSLF GLLNHCKTPV GSRLLAQWLK QPLMDLAEIE KRQQLVEAFV
     VNTELRQTMQ EEHLRSIPDL YRLAKRFQRK QANLEDVVRV YQVAIRLPGF VNSLENVMDE
     EYQTPLETEY TSNLRSHSDS LAKLEEMVET TVDLDALENH EFIIKPEFDE SLRIIRKKLD
     KLRHDMGVEH RRVARDLDQD IEKKLFLENH RVHGWCFRLT RNESGCIRNK REYQECSTQK
     NGVYFTTSTM QTLRREHDQL SSNYNRTQTG LVNEVVNVAA SYCPVLERLA GVIAHLDVIV
     SFAHASVHAP TPYARPKMHP RGTGNTVLKE ARHPCMEMQD DISFITNDVA LVRDESSFLI
     ITGPNMGGKS TYIRQIGVIA LMAQTGCFVP CTEAELTIFD CILARVGASD SQLKGVSTFM
     AEMLETSNIL KSATSESLII IDELGRGTST YDGFGLAWAI SEHIVTEIRC FGLFATHFHE
     LTALADRYPK SVKNLHVVAF IGDGTDDDSE DKKSKRNQVT LLYRVEPGIC DQSFGIHVAE
     LVRFPEKVVN MARQKAEELE DFTSSEQQDQ QSSMAIDKYS QEEVEEGSAL LKAMLLKWKS
     ETESSGKELT VEEKRQIMRD LVKADEKLQA NKVFQGIKAL
//
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