ID A0A0D2D1A8_9EURO Unreviewed; 1245 AA.
AC A0A0D2D1A8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA mismatch repair protein {ECO:0000256|PIRNR:PIRNR037677};
GN ORFNames=PV06_10706 {ECO:0000313|EMBL:KIW37078.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW37078.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW37078.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW37078.1,
RC ECO:0000313|Proteomes:UP000053342};
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 oligosperma CBS72588.";
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; KN847346; KIW37078.1; -; Genomic_DNA.
DR RefSeq; XP_016257294.1; XM_016412280.1.
DR AlphaFoldDB; A0A0D2D1A8; -.
DR STRING; 215243.A0A0D2D1A8; -.
DR GeneID; 27362780; -.
DR VEuPathDB; FungiDB:PV06_10706; -.
DR HOGENOM; CLU_002472_1_0_1; -.
DR OrthoDB; 168255at2759; -.
DR Proteomes; UP000053342; 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 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:UP000053342}.
FT DOMAIN 1071..1087
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 246..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..195
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 138759 MW; 434E9BA6EA3BB536 CRC64;
MPPKKTPLGP ASTPSLKKSQ SSGSGQKTLL GFFQRTPSTG SSPALPSRQS TATPGLQKDR
ERSTAAYSTS SLTPIPSSDG PEPELDKDKG DDVRTSPPPA KGLPSPVSAD ERQTNGVGDS
SARGTPSRRA KKIINYIESD SEGTDGDDVF KPKAAVRSRP VKRRRLSDSA DEDVYQQENE
VAQSEDDMDD FIVPDDSDDD VRRPVKRKRP SKPVARKTSS HFTPVEDEVD EPVDVAFDAD
MDLPEGSTAQ KWTYDPENPQ PLQLRPSNIP SKKPGKQKAH MTEPEQRHAW LEDVRDMDRN
PPGHPDYDPR TLYIPPMAWA KFSPFEKQYW EIKQKFWDTI VFFKKGKFYE LYENDATIGH
QLFDLKLTDR VNMRMVGVPE SSLGLWANQF VAKGFKIARV DQQESKLAKD MRERAEKDAS
EDSMSGFGGR KGASKWAKGG SAASKKDDKV IKRELACVLT AGTLVDGTML QDDMATYCVA
IKEAEVDGLP SFGVAFVDTA TGHFHIAEWI DDADLTRFET FVAQTRPQEL LLEKGGISTK
TLRILKNNTG LTTIWNYLKP GKEFWEGHIT AKEIEACDYF PMDWPEVLQQ AREKDLLMSA
LGALIQYLRT LKIERELVTL GNFTWYDPIR KAGSLVLDGQ TLINLEVFAN SYDGGPEGTL
FQLLNRCITP FGKRMFKQWV CHPLMDTKKI NARLDAVDSL NADTKVRDRF TSQMSKMPDL
ERLISRVHAG ACRVQDFVSV LEGFEQIDHT MSLLRDGSGR PQDAEGVIGQ LISAMPDLES
RLKYWTDAFD RSKAKETGVL VPERGFEEDF DNSHDLIEEI QQEFNVLLRK WRKELGSSAI
CYRDNGKEIM QLEVPTKVKG IPKNWDQMSA TQAVKRYYFP ELRALVRKLQ EAQETHAQIS
KEVTRRFQAR FDENYEIWLA AVKVIAQLDC LISLAKASAS LGYPSCRPEF VDDDDHTRST
LELVELRHPC LLAKVDNFIP NDVVLGGDEA NISLLTGANA AGKSTVLRMT CIAVIMAQVG
CYLPCQSARL TPFDRIMSRL GAQDHIFAAQ STFFVELAET KKILSEASPR SLVILDELGR
GTSSHDGVSV AQAVLHHLAS HVGCLGFFAT HYHSLSAEFK GHPQIIPQRM SILVDDENRR
VTFLYKLESG TAEGSFGMHC ASMCGIAPGI VDRAEEAAKQ WEYTSLMARR LKGGAGTEDG
EDGQGKEREV PLGLLSDLAW MLNEERGGEI CDGGIDALVK CIEAL
//
