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MUTS2_CLOBB
ID   MUTS2_CLOBB             Reviewed;         785 AA.
AC   B2TS45;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=CLL_A2463;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001056; ACD24590.1; -; Genomic_DNA.
DR   RefSeq; WP_012425331.1; NC_018648.1.
DR   AlphaFoldDB; B2TS45; -.
DR   SMR; B2TS45; -.
DR   PRIDE; B2TS45; -.
DR   EnsemblBacteria; ACD24590; ACD24590; CLL_A2463.
DR   KEGG; cbk:CLL_A2463; -.
DR   PATRIC; fig|935198.13.peg.2423; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000001195; 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; PS50828; SMR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding.
FT   CHAIN           1..785
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093347"
FT   DOMAIN          710..785
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   785 AA;  88203 MW;  764A21293AAAF792 CRC64;
     MNKRSLRVLE FNKVKEILKK YAYSSSAKKL VDELVPYDNT YEINNSLEES NEALEILMKK
     GNPPIEGLCD IGDILQRAKK GGTLTPEQLL KVLGMLTATR RMQEFFKREE QEVSFPKLED
     LAYILAPIND LEKEIERSIL SEDEVSDNAS TTLYNIRRSL KEKNSSVREK INSIVRSNSK
     YLQDSLYTIR GDRYVIPVKA EYKSSVPGLV HDQSSTGATL FIEPMGLVNL NNEIKELMLK
     EKAEIDRVLS ALSLKVKMNA EHCESNLKIL TNLDFIFSKG KYACELNAIK PMVRDDGIFN
     IMSGRHPLIE KDKVVPLDVV LGDEFDTLMI TGPNTGGKTV TLKTVGLLHI MALSGLLIPA
     SSNSSVSFFK EVFADIGDEQ SIEQSLSTFS SHLTNIVNIM EYDNRQSLIL FDELGGGTDP
     AEGAALAIAI IENLSSKGAK LIATTHYSEL KAYALNKDRV ENASVEFDIN TLRPTYRLLI
     GVPGKSNAFE ISKRIGLGKE VIDCAKNYMS KENLEFEGLI RNLQEKSIIA KKDARDAKVI
     KDEADNLKKK YEQKLERLEK VKDKAYMEAR EEAKKIVANA KDEADEILKA MRELEKLGIG
     SGGRQRLEEE RKKLKDSLEE KEKNLYKMKE NDGEVLEKVA LGMEAFLPSL NQTVVVISMP
     DNRGEVQVEA GIMKISVKLK DLRKTKQSKV EKVKKKRELK LHFSKVENRI DLRGLDAEEA
     CYRVDKYLDD AYMGNLGEVT IVHGKGTGIL RKAINDMLKR HVHVKNYRLG GYGEGGDGAT
     IVELK
 
 
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