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MUTS2_LACJO
ID   MUTS2_LACJO             Reviewed;         788 AA.
AC   Q74KU8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=LJ_0479;
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533;
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT   johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS08471.1; -; Genomic_DNA.
DR   RefSeq; WP_011161611.1; NC_005362.1.
DR   AlphaFoldDB; Q74KU8; -.
DR   SMR; Q74KU8; -.
DR   STRING; 257314.LJ_0479; -.
DR   EnsemblBacteria; AAS08471; AAS08471; LJ_0479.
DR   KEGG; ljo:LJ_0479; -.
DR   PATRIC; fig|257314.6.peg.506; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000000581; 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; Reference proteome.
FT   CHAIN           1..788
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093366"
FT   DOMAIN          713..788
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         334..341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   788 AA;  88493 MW;  7AB4DA60769D36E3 CRC64;
     MNSKIIEKLE YNRIIKQLSD LAITVPAKEQ ALTLMPSSNF DEVKKSIDQT RVLSNVLRVK
     GPMPITDFKD VRASLKRLKV KANLNGEELG NIFLILSLAK DVSQFTADLE EREIDTRPIE
     KTLKNLAIPE DLFKKLNQAI EYDGTVKDTA SSKLMQLRHD IQSNETDIKN HMNDYISGKH
     TQYLSENIVT IRDGRYVLPV KQEYKNKFGG VVHDQSASGQ TLFVEPQAVL VLNNRQQNLM
     AQERQEIHRI LIELSELAGM YQKEIKNNAD ALTQLDFLSA KSKLAKAMKA TEPVLNQDHV
     IKLRKARHPL IDPKKVVPNN IELGTSFDTM LITGPNTGGK TITLKTLGLL QLMAQAGLFI
     TAEEGSQLTV FNEIYADIGD EQSIEQSLST FSSHMDQIIK IMKDVTEDDL VLIDELGAGT
     DPEEGASLAI AILDDLRGAQ AKIAITTHYP ELKLYGYNRA RTTNASMEFD LKKLAPTYRL
     RIGIPGQSNA FAIAHQLGMN EVVVDKARSL MNDEDSDINK MIERLTEQTK AAEQLHETLK
     QNVDQSITLK RQLQNGLDWY NQQVQKQLEK AQEKADEMLA KKRQKADKII NDLEEQRRAG
     GQVRTNKVIE AKGALNKLER ENQNLAQNKV LQREKRRHDV SVGDTVKVLS YGQQGVITKK
     LADHEFEVQI GILKVKVTDR DVEKISTQAA PKKAERAVRS SRDLRSTRAS SELDLRGQRY
     EEALTNLDRY IDSSLLAGLN TVTIIHGIGT GAIRNGVQQY LKRNRHVKSY SYAPANQGGT
     GATIVYLQ
 
 
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