位置:首页 > 蛋白库 > MUTS2_LISMF
MUTS2_LISMF
ID   MUTS2_LISMF             Reviewed;         785 AA.
AC   Q720J7;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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};
GN   OrderedLocusNames=LMOf2365_1241;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(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}.
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; AE017262; AAT04017.1; -; Genomic_DNA.
DR   RefSeq; WP_010958871.1; NC_002973.6.
DR   AlphaFoldDB; Q720J7; -.
DR   SMR; Q720J7; -.
DR   KEGG; lmf:LMOf2365_1241; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
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   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..785
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_0000115225"
FT   DOMAIN          710..785
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         335..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   785 AA;  86509 MW;  C404D1DD03E389A2 CRC64;
     MEKKVEAILE FDKIKKQLTE FASSSLGEQA ILELAPATDF QVVQKTQLET EEGAKIIRLR
     GSAPITGLTD VFAHLKRLEI GGDLNGLEIY QIGSNLRVSR QMKNFMNDLL EIGVELPLLG
     ALSDELLVLK EVEEDIAISV DESGKVLDTA SEALSTIRRT LRRTEDRVRE KLESYLRDRN
     ASKMLSDAVI TIRNDRYVIP VKQEYKGHYG GIVHDQSASG QTLFIEPQSV VDLNNERKAL
     QAKEKQEIER ILAEISASLA AWINEIHHNT FILGRFDFIF AKARFGKAMK AVTPHLSDAG
     VVHLIAARHP LLDAAKVVAN DIYLGEDFTT IVITGPNTGG KTITLKTLGL LTLMAQSGLQ
     IPAQEDSTIA VFEHVFADIG DEQSIEQSLS TFSSHMTNIV SILGNVNQKS LILYDELGAG
     TDPQEGAALA IAILDASHAK GASVVATTHY PELKAYGYNR VHATNASVEF NVETLSPTYK
     LLIGVPGRSN AFDISRRLGL SENIITEARS LVDTESADLN DMISSLEEKR NLAETEYEEA
     RELARGAGNL LKDLQKEISN YYQQKDKLIE QASEKAATIV EKAEAEAEEI IHELRTMQLN
     GAAGIKEHEL IDAKTRLGNA KPKTINKTIP QAPKQKPHVF QEGDNVRVLS LGQKGTLLNK
     ISDKEWNVQI GIIKMKIKTV DLEYIQPEKP KKQRIITSVH SSGSPAKSEL DLRGERYEDA
     LQKVDKYLDE ALLAGYPQVA IIHGKGTGAL RTGVTEYLKN HRMVKSIRFG AAAEGGNGVT
     IVEFK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024