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MUTS2_THERP
ID   MUTS2_THERP             Reviewed;         792 AA.
AC   B9KYW4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=trd_0668;
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC   Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC   Thermomicrobium.
OX   NCBI_TaxID=309801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA   Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA   Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
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; CP001275; ACM06343.1; -; Genomic_DNA.
DR   RefSeq; WP_012642064.1; NC_011959.1.
DR   AlphaFoldDB; B9KYW4; -.
DR   SMR; B9KYW4; -.
DR   STRING; 309801.trd_0668; -.
DR   EnsemblBacteria; ACM06343; ACM06343; trd_0668.
DR   KEGG; tro:trd_0668; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_0; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000000447; 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.
FT   CHAIN           1..792
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000118574"
FT   DOMAIN          716..791
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         344..351
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   792 AA;  87887 MW;  CBFA792CB36B1D16 CRC64;
     MASELLRLLE FDKIRELLAA RCQYSVASER AREIAPTADR DQVAYLLRVT REAARLLNER
     PSFTIGGFRD IRSVVQAAQR GNILAPADVR TVLDTLEAAA SLRRQFMADE RWSERYPALA
     EFVLAMVDLP GLRADLARSI GPRGEVLDTA SPELAAIRRS LKEAHERLLE RLRRLLAERQ
     EAIQDAYVTI RDGRYVIPVR ADRRQAVPGI THDVSGSGQT LFVEPFEVLE LNNRWRELQA
     AETREIERIL RVLTQRIADA ADELLQIVEA GAALDLALAK ARLAYDLDAV EPELLEPSGP
     TVPEGHPFLR VRLRAARHPL LDRRTAVPID VELGERFRIL VITGPNTGGK TVALKTVGLL
     ALMAQAGLFI PAAPGSGLSV FPAIFVDIGD EQSIEQNLST FSSHMRRIVA TLQQADASSL
     VLLDEIAAGT DPQEGAALAR AILERLLEIG ALGIVTTHYP ELKVFATGTP GLENASVEFD
     PVTLSPTYRL LVGLPGRSHA LEVARRLGLP EDVIARAREL LGSGAPQLDR LIAEMQRRLE
     EAESLAAAAE RSRREAEQLR AAAERLLAEA ERERREARQE VLRELEAELA RARELARKIE
     RAARSPAYPP IEVTQDSLRA LEEVKRRVQS SGRQSRQERV PEIAVGDRVE LTALGLEGDV
     VAIHPESEEV EVRIGQFRVR QPQASVRRIW PRREEVSQTF APPVSVTTIP RVEPEIHLRG
     LHVEEALDRL DRYLDRAVRA GLPWVRVVHG KGTGTLRQAI HAFLRDHPLV KSWELAGPHE
     GGLGVTVVYL EV
 
 
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