ID A2R8R7_ASPNC Unreviewed; 950 AA.
AC A2R8R7;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 86.
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=An16g08110 {ECO:0000313|EMBL:CAK47060.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK47060.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK47060.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(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. {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}.
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DR EMBL; AM270376; CAK47060.1; -; Genomic_DNA.
DR AlphaFoldDB; A2R8R7; -.
DR EnsemblFungi; CAK47060; CAK47060; An16g08110.
DR VEuPathDB; FungiDB:An16g08110; -.
DR HOGENOM; CLU_002472_4_0_1; -.
DR Proteomes; UP000006706; Chromosome 5R.
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; 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; 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:SF34; DNA MISMATCH REPAIR PROTEIN MSH1, MITOCHONDRIAL; 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; PF00488; MutS_V; 1.
DR PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 2.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR SUPFAM; SSF53150; DNA repair protein MutS, domain II; 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};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 819..835
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 930..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 105981 MW; 37123350A231AB65 CRC64;
MSSCPATVHA PAQDLPQGAL KLQPYQEVVD DAPKYPAVVQ GHWNNMQKFK NCVILTRVGG
FYELYFEQAE EFAPLLNLKL ASKKTSAGPV PMAGFPFFQL DRFLKILVQD LNKYVAVSEE
FPNAAEDKLR SGGLLFDRKV ARIITPGTLI DEKFMDPSEN NFLLAVYIDK SSLKEQLMQQ
DASSSQQHVL LSASQNVGLS WLDLSTGDFF TQVTTAQMLP SAIARIGARE ILVDQGLQDV
IGQELQLLIG HDQRLMTFFQ FPKKVAPMAR WEAMLEAPVS DAAAETFTRE EVAAGYSLLE
YIRVQLQGLN MKLQPPRRRH LDESMSIDRN SLRGLEILET ARDGFGKGSL LHAVRRTSTK
SGARLLRDRL TSPSTSLSVI NERLDLVSIF IEDRDLHDNV IQFLKRSYDA QRLVQKFTLG
RGDPDDLICL SRAIEASKEI RQVLSRKWHS EADSQTKRSI GIMVDRIHMD GPTVLADKIL
TAIDEEGLLQ KQRIEDDTAA EAALLAQSVT LNEGIPEDMA ALPKKVKTKS SDRSSASTDE
GTIADTWIMR RDASPALSEL HQDLEQLHTA KSELTQRLRE SVGSSALTLK WTPGLGHICH
VKGARITQES LEELGVTRNV SSTKSTRSFY LPAWTELGGQ MDQVKTQIRQ EEQVIFEHLR
REVILNLVKI RRNAAVMDEL DVACSFATLA QEQQLVRPIL NEDKSHKIVG GRHPTVKLGL
EEQGRRFVSN DCFLGGPERI WLVTGPNMAG KSTFLRQNAL ITILAQVGSF VPAAYAEIGL
VDQIFSRIGA ADDLFRDQST FMVEMLETAA ILKQATSRSF VIMDEVGRGT TPEDGTAVSF
ACLHHLHYHN KCRTLFATHF HVLADMTHDF DALGRYCTDV KESASGSFSF IHRLRKGVNR
ESHALKVAQL AGLPREAIEM AKNVRQRFAN HNDSPHWDEN SAPKHTANGA
//
