ID A0A179V0W9_BLAGS Unreviewed; 1162 AA.
AC A0A179V0W9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA mismatch repair protein {ECO:0000256|PIRNR:PIRNR037677};
GN ORFNames=BDBG_09053 {ECO:0000313|EMBL:OAT13945.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT13945.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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. MSH3
CC subfamily. {ECO:0000256|ARBA:ARBA00007094}.
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DR EMBL; GG657481; OAT13945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A179V0W9; -.
DR STRING; 559298.A0A179V0W9; -.
DR VEuPathDB; FungiDB:BDBG_09053; -.
DR OrthoDB; 168255at2759; -.
DR Proteomes; UP000002038; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:UniProtKB-UniRule.
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; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361:SF122; DNA MISMATCH REPAIR PROTEIN MSH3; 1.
DR PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR Pfam; PF01624; MutS_I; 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; 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, ECO:0000256|PIRNR:PIRNR037677};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR037677};
KW DNA repair {ECO:0000256|PIRNR:PIRNR037677};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037677};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037677};
KW Reference proteome {ECO:0000313|Proteomes:UP000002038}.
FT DOMAIN 1005..1021
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 1..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1162 AA; 127974 MW; A747998CD3D647B1 CRC64;
MSSSQSSSQL KRKQQSISSF FAKKPVPVNG STNATPKNGA GKKLGEARVR QTPDSEVNEV
VNGGYGAGGM EKEEEEDDEI IVPSRKRIRS NGDVSTVHRG APADADQRRD VKETDTGMDM
GVVDEFDSDG VMKLPTAKKE KNTGSARTER FRFNSSATPT SSDQRADGNG GDASEDDERE
RKRKQALHQK FVKRLGGPDC LPPLTSGFGA GDADDLEGAE SDAEAEEDVA PAPQKVRGAG
KRTTTGKLTP MERQIIDIKK NHMDTVLVVE VGYKFRFFGE DARIAAKELS IVCIPGKLRF
DEHPSEAHLS RFASASIPVH RLHVHVKRLV AAGYKVGVVR QLETAALKAA GDNRNAPFVR
KLTNLYTKGT YIDDVEGLEG PSVSSGSAST STGYLLCMTE SNAKGCGNDE KVHVGIVAVQ
PATGDVIYDD FEDGFMRSEI ETRLLHIAPC EFLIVGEMSK ATEKLVQHLS GSKTNVFGDK
VRVERVSKSK IAAAESHSHV SSFYAGRMKA KGAVGDAAAN NLLEKVLKLP EDVTICLSSM
IKHMSEYGLE YIFDLTKYFQ PFSARSHMLL NGNTLTNLEI YQNQTEHTSK GSLFWTLDRT
KTRFGQRLLR KWVGRPLLDK SELEERVAAV EELQDPSKTV QIERLKGLLS KIKADLEKSL
IRIYYGRCTR PELLTVLQTL QLIADEYVHL KSPEDLGFSS PTINRAIAAL PAIRKDVVTY
LNKINAQAAK KDDKYCFFRE AEETDEITES NLGIADVQHR LKEHCAVAAE ILGKKKVQYT
TVAGIEYLIE VENSPYNLKK VPASWRKISG TKKVSRFHTP EVVQYMRERD QYKEALAAAC
DKAFHALLAD ISTKYQSFRD CIVALATLDC LLSLANIASQ PGYVKPTYTD ETRISVQRGR
HPMVEQLLLD SYVPNDIELH TNKTRALLVT GPNMGGKSSY VRQVALICIM GQIGSYVPAE
SATLGMLDAV YTRMGAFDNM LAGESTFMVE LSETADILKQ ATPRSLVILD ELGRGTSTHD
GVAIAQAVLD YMVRNLRSLT LFITHYQNLS SLAREFPKGE LRNVHMKFTE SGMDGRDITF
LYEVGEGVAH RSYGLNVARL AHVPTSVLDV ARTKSAELEE KIRKKKLLAL AKVVKGAIDT
DGAAREVDAA LLEGVFVGLE QL
//
