位置:首页 > 蛋白库 > MUTS2_CLOB8
MUTS2_CLOB8
ID   MUTS2_CLOB8             Reviewed;         786 AA.
AC   A6LS00;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Cbei_0946;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000721; ABR33130.1; -; Genomic_DNA.
DR   RefSeq; WP_011968289.1; NC_009617.1.
DR   AlphaFoldDB; A6LS00; -.
DR   SMR; A6LS00; -.
DR   STRING; 290402.Cbei_0946; -.
DR   EnsemblBacteria; ABR33130; ABR33130; Cbei_0946.
DR   KEGG; cbe:Cbei_0946; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000000565; 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..786
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093345"
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   786 AA;  88384 MW;  79359CE7F3F4C2D6 CRC64;
     MNERSLRILE FNKIKEKIKK YARTNAAKAK VEDLEPYDNL YEINNKLEET NEALEILISK
     GNPPLEGLAD IHEGIERAKK GGTLSPGQLL KVGGMLKATR NMKEFFKREE VEKSYPKLED
     LAYILAPVKA LEDEIERAIV SEDEISDKAS QTLCNIRRSL KEKNSSVREK ISSIVRSNSK
     YLQDDLYTMR GDRYVLPVKS EYKSQVPGLV HDQSSTGATF FIEPMSLVNL NNEIRELFLK
     EKAEIERILS DLSLKVKING DSCLSNLKVL VEFDFIFAKG RYASALNAIK PIVREDGAFS
     IFSGRHPLIE NDKVVPSDIY LGEEFQTLMI TGPNTGGKTV TIKTVGLLHI MGLSGLLIPA
     RDNSSIAFFK EIFADIGDEQ SIEQSLSTFS SHMTNIVNIM KHVDDKSLAL FDELGAGTDP
     AEGAALAVSI LETLRNRGAK LIATTHYSEL KAYALKTDGV ENASVEFDIE TLRPTYRLLI
     GVPGKSNAFE ISKRLGLVEG VIKRAKEYMS EENLQFENLI RELQEKSIIA KKEAREAKML
     RDQAEDLKKK YEEKLEKLEN TREKAYMDAR REAKEIIANA KDEADDILKA MRELEKLGIA
     GGGRQRLEEE RKKLKDSLEE REKGIHKMKE NEGESITNVT LGMEAYLPSL NQKVIIVSMP
     DNRGEVQVEA GIMKVNVKLK DLRKTQVTKE EKVRRKREVK LNLSNVESRV DLRGLDAEEA
     CYKADKYLDD AYMANLGEVT IVHGKGTGVL RKAINDMLKR HPHVKSYRLG AYGEGGDGVT
     MVELKG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024