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MUTS2_FUSNN
ID   MUTS2_FUSNN             Reviewed;         778 AA.
AC   Q8RIK8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=FN1581;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(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; AE009951; AAL93696.1; -; Genomic_DNA.
DR   RefSeq; NP_602397.1; NC_003454.1.
DR   AlphaFoldDB; Q8RIK8; -.
DR   SMR; Q8RIK8; -.
DR   STRING; 190304.FN1581; -.
DR   EnsemblBacteria; AAL93696; AAL93696; FN1581.
DR   KEGG; fnu:FN1581; -.
DR   PATRIC; fig|190304.8.peg.73; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_0; -.
DR   InParanoid; Q8RIK8; -.
DR   OMA; IHAIIND; -.
DR   BioCyc; FNUC190304:G1FZS-85-MON; -.
DR   Proteomes; UP000002521; 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:0003690; F:double-stranded DNA binding; IBA:GO_Central.
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..778
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093359"
FT   DOMAIN          703..778
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   778 AA;  88646 MW;  65D221D2015C2545 CRC64;
     MNKHSFNVLE FDKLKELILA NIVIDHNREV IENLEPYKDL SALNNELKTV KDFMDLLSFD
     GGFEAIGLRN INSLMEKIKL IGTYLEVEEL WNINVNLRTV RIFKSRLDEL GKYKQLREMI
     GNIPNLRVIE DVINKTINPE KEIKDDASLD LRDIRLHKKT LNMNIKRKFE ELFEEPSLSN
     AFQEKIITER DGRMVTPVKY DFKGLIKGIE HDRSSSGQTV FIEPLSIVSL NNKMRELETK
     EKEEIRKILL RIAELLRNNK DDILIIGEKV MYLDILNAKS IYAVENRCEI PTVSNKEILS
     LEKARHPFID KDKVTPLTFE IGKDYDILLI TGPNTGGKTV ALKTAGLLTL MALSGIPIPA
     SENSKIGFFE GVFADIGDEQ SIEQSLSSFS AHLKNVKEIL EAVTKNSLVL LDELGSGTDP
     IEGAAFAMAV IDYLNEKKCK SFITTHYSQV KAYGYNEEGI ETASMEFNTD TLSPTYRLLV
     GIPGESNALT IAQRMGLPES IISKAREYIS EDNKKVEKMI ENIKTKSQEL DEMRERFARL
     QEEARLDRER AKQETLIIEK QKNEIIKSAY EEAEKMMNEM RAKASALVEK IQHEEKNKED
     AKQIQKNLNM LSTALREEKN KTVEVVKKIK TKVNFKVGDR VFVKSINQFA NILKINTSKE
     SAMVQSGILK LEVPFDEIKI VEEKKEKVYN VNNHKKTPVR SEIDLRGKMV DEAVYELETY
     LDRATLNGYT EVYVIHGKGT GALREGILKY LKACKYVKEY RIGGHGEGGL GCTVVTLK
 
 
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