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MUTS2_CLOPE
ID   MUTS2_CLOPE             Reviewed;         786 AA.
AC   Q8XJ80;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Endonuclease MutS2 {ECO:0000255|HAMAP-Rule:MF_00092};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00092};
GN   Name=mutS2 {ECO:0000255|HAMAP-Rule:MF_00092}; OrderedLocusNames=CPE1881;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC   -!- FUNCTION: Endonuclease that is involved in the suppression of
CC       homologous recombination and may therefore have a key role in the
CC       control of bacterial genetic diversity. {ECO:0000255|HAMAP-
CC       Rule:MF_00092}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00092}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00092}.
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DR   EMBL; BA000016; BAB81587.1; -; Genomic_DNA.
DR   RefSeq; WP_011010657.1; NC_003366.1.
DR   AlphaFoldDB; Q8XJ80; -.
DR   SMR; Q8XJ80; -.
DR   STRING; 195102.gene:10491146; -.
DR   PRIDE; Q8XJ80; -.
DR   EnsemblBacteria; BAB81587; BAB81587; BAB81587.
DR   KEGG; cpe:CPE1881; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IEA:InterPro.
DR   CDD; cd03280; ABC_MutS2; 1.
DR   Gene3D; 3.30.1370.110; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00092; MutS2; 1.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR005747; MutS2.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002625; Smr_dom.
DR   InterPro; IPR036063; Smr_dom_sf.
DR   PANTHER; PTHR11361; PTHR11361; 1.
DR   PANTHER; PTHR11361:SF14; PTHR11361:SF14; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   Pfam; PF01713; Smr; 1.
DR   PIRSF; PIRSF005814; MutS_YshD; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SMART; SM00463; SMR; 1.
DR   SUPFAM; SSF160443; SSF160443; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01069; mutS2; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   PROSITE; PS50828; SMR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..786
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_0000115220"
FT   DOMAIN          711..786
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         332..339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   786 AA;  88111 MW;  74A606E8521314B7 CRC64;
     MNDRVLRVLE FNKIKELVKG YAITKSAKEM VLDLKPYDSV YDVKEHLEET KEALDILMRK
     GNPPFEGLYD VKEAITRAEK GGVLSIEGLL RIGNMLAVTR KLSDFLARKE EEEEHRILEG
     MREGLIVLRG VESAISKAIV SEDEIADSAS DKLYSIRRSL KEKNSSIRDK VNSIVRSNTQ
     YLQDSLYTVR GDRYVIPVKA EYKSQVPGLV HDQSSTGATL FIEPTALVNL NNEIKELMLK
     ERAEIERILA ELSVLVYKNI DVIKVNFNII VELDFIFAKA KYGSDLGGTL PIVNEEGVID
     LMDARHPLIP KDKVVSSDIY LGREFSTLLI TGPNTGGKTV TLKTTGLIEL MGLSGLLIPA
     SENSSISFFE EIFADIGDEQ SIEQSLSTFS SHMTNIVRIM EKANNKSFVL FDELGAGTDP
     TEGAALAISI LENLRARGCR IMSTTHYSEL KGYALKTENV ENASVEFNVE TLRPTYRLLI
     GVPGKSNAFE ISRRLGLKDN VIEEAKKVIS TESLQFEDLI QSLQEKSIKA ENDAREAAIL
     RNDAEKYKNR YKEKFERIES VRDNVYADAR REAKQILDSA KEEADAILKN MRDLERMGIS
     SDARRKLEAE RGKLRDKISD AEARLQKKKE EQKGEELKKI EVGMEALLPS INQKVIVLSK
     PDNKGEVQVQ AGIMKINVKA KDLRVAKETK EEKKIKKREA RLNLRQVDPS IDLRGMDSEE
     ACYTADKYLD DAYVAGRGEV TLVHGKGTGV LRKAINDMLK KHPHVKSHRL GEYGEGGTGV
     TVVILK
 
 
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