ID A0A093VE23_TALMA Unreviewed; 1211 AA.
AC A0A093VE23;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=DNA mismatch repair protein {ECO:0000256|PIRNR:PIRNR037677};
GN ORFNames=GQ26_0132750 {ECO:0000313|EMBL:KFX48239.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX48239.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX48239.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX48239.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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|PIRNR:PIRNR037677, 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:KFX48239.1}.
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DR EMBL; JPOX01000013; KFX48239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093VE23; -.
DR eggNOG; KOG0217; Eukaryota.
DR HOGENOM; CLU_002472_1_0_1; -.
DR Proteomes; UP000029285; 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; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 1033..1049
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 1..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 136075 MW; 5CF5E3D835B46025 CRC64;
MAKGSGAASS PPAASTPALK RSTSSTQNMK NQRSILGFFQ KSSPATPSTA PRKAPPPAEP
ASSPAQRAAD TKSSIKKKPA QNLTPAPSSD VIEPDEDDSA TPKVSKNAQD DQSLTPSRRT
KKKVNYMESD SEGVDDDEEI FRPQPSRKRR RPAIESEDEF QDDGKDAHMS EDEMDDFIVD
ESEEDARPNK KRKKAAARPA QRSKSSTEEP VRPADADFDL DIPEATAGGT AQKWTYDPEN
TEPRQERQQR EPSSNGTTKR KEKAHETEPE KRYPWLANIM DMDKNPPGHP DYDPRNIYIP
PLAWSKFSPF EKQYWEIKQK FWDTIVFFKK GKFYELYEND ATIGHQLFDL KLTDRVNMRM
VGVPEMSLDH WANQFVAKGY KIARVDQSES ALGKEMRERD DKKAKVGKED KIIKRELACV
LTAGTLVEGS MLQDDMSTYC VAIKEIILDG LPAFGIAFVD TATGQFYLSE FKDDADMTKF
ETFVAQTRPQ ELLLEKSAVS QKAMRILKNN TGPTTLWNHL KPGKEFWEAD IAVRELDASD
YFVSPDSDNI NAWPQVLREA REKENAMSAF GALVQYLRVL KLDRDLISIG NFTWYDPIRK
ATSLVLDGQT LINLEIFANS FDGGSEGTLF QLLNRCITPF GKRMFKQWVC HPLVDIDKIN
ARFDAVDALN ADSTIRDQFS SQLTKMPDLE RLISRIHAGA CKGQDFLRVL EGFEQIEYTM
GLLKDLGSGE GLIGKLVSSM PDLVSPLEYW KTAFDRLKAK ENGILVPEQG IEEDFDASQA
TIEQIHRDLE NLLKQARRDL GSTAICYRDN GKEIYQLEVP IKVKNIPKTW DQMSATKQVK
RYYFPELRAL IRKLQEAQET HSQIVKEVAG RFYARFDEDY ETWLKSIRIV AQLDCLISLA
KASSSLGQPS CRPEFVDSER SVLEFEELRH PCMLQNVTDF IPNDVQLGGD KASINLLTGA
NAAGKSTILR MTCVAVIMAQ VGCYIPCQSA RLTPVDRIMS RLGANDNIFA AQSTFFVELS
ETKKILSEAT PKSLVILDEL GRGTSSYDGV AVAQAVLHHI ATHVGSLGFF ATHYHSLAAE
FENHPEISPK RMRIHVDDEE RRVTFLYKLE DGVAEGSFGM HCASMCGIPN KVIENAENAA
KQWEHTSRLT ESLERRKGGG LVGLGWWSDV AWMLREGDNV DVSDRGLEIL RKAIETLRTA
GKRRASPIET T
//
