ID A0A0D1VPT3_9EURO Unreviewed; 1225 AA.
AC A0A0D1VPT3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA mismatch repair protein {ECO:0000256|PIRNR:PIRNR037677};
GN ORFNames=PV11_09856 {ECO:0000313|EMBL:KIV78100.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV78100.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV78100.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV78100.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) 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 -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000256|PIRNR:PIRNR037677, ECO:0000256|RuleBase:RU003756}.
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DR EMBL; KN846954; KIV78100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1VPT3; -.
DR STRING; 1016849.A0A0D1VPT3; -.
DR OrthoDB; 168255at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
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; 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:SF148; DNA MISMATCH REPAIR PROTEIN MSH6; 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; PIRSF037677; DNA_mis_repair_Msh6; 1.
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, ECO:0000256|PIRNR:PIRNR037677};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR037677};
KW DNA repair {ECO:0000256|PIRNR:PIRNR037677, ECO:0000256|RuleBase:RU003756};
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:UP000053599}.
FT DOMAIN 1054..1070
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 786..813
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1225 AA; 137070 MW; 43D022D0B2B74073 CRC64;
MPKKSAANPA STPALKKTPS SGGQRTLLGF FSKTPSSGSP AGLPALPAKK TTTNPALPKN
GSKATGRTSG SSLTPVPSSE GPEPEYEDED NKASSPPARG LPSPVSADEG QTNGLDELNA
RGTPSRRAKH KTISYVESDS EGTDDDVFKP KPVARARPTK RRRLSHSADE DVYQQENEVE
QEDDEMDDFI APDDSDDDVK PSHKRKRPTK AASRKVSSHF THSTDADAGG VGMDIDLDLD
LPDTSTAQKW TYDPENPQPL QPRSSNIPSK EPGSKKQKAH MTEPEQRHAW LQDIRDIERN
KPDHPDYDPR TLYIPPMAWI KFSPFEKQYW EIKQKFWDTI VFFKKGKFYE LYENDATIGH
QLFDLKLTDR VNMRMVGVPE SSLGLWANQF VAKGFKIARV DQLESKLAKD MRERDEETST
KTSTKKPSKD DKVVKRELAC VLTAGTLVDG TMLQDDMSTY CVAIKESEID DLPAFGIAFV
DTATAQFHIT QFTDDADMTK FETFIAQTRP QEILLEKGGV STRTLRILKN NTGPTTIWNY
LKPGKEFWEG HITAKEIEAC DYFPMDWPEA LEQSKDKDLL MSALGALIQY LRTLKIERDL
VTLGNFTWYD PIRKASSLVL DGQTLINLEI FANSFDGGVE GTLFQLLNRC ITPFGKRMFK
QWVCHPLMDT KKINARLDAV DSLNADTKVR DRFTSQMTKM PDLERLISRV HAGTCKVQDF
VRVLEGFEQI DHTMSLLRDG SGKPQDSEGV IGQLISAMPE MESILKYWMD AFDRKKAKDT
GVLVPERGVE EDFDESQDNI EAIQEEFNVL LRQWRKELGS SAICYRDNGK EIMQLEVPMK
VKGIPKNWDQ VSATQAVKRW YFPELRALVR RLQEAQETHS QIVNQVARRF FARFDENYDV
WLAAVRIIAQ LDCLISLAKA STSLGHPSCR PEFIESDDST RSTLELVELR HPCLLTMVDD
FIPNDVVLGG DTANISLLTG ANAAGKSTVL RMTCIAVIMA QIGCYLPCQS ARLTPFDRIM
SRLGAQDHIF AAQSTFFVEL AETKKILSEA TPRSLVILDE LGRGTSSHDG VAVAQAVLHH
LASHIGCLGF FATHYHSLSA EFKGHPEIVA QRMKILVDDE NRRVTFLYKL EPGTAEGSFG
MHCASMCGIA PVVVDRAEEA ARKWEYTSLM ARRLNAGELE GDEAEKEREV SLGILSDLAW
MLDEEKGEVV SERGIEALVK CIEGL
//
