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MUTS2_CLOPS
ID   MUTS2_CLOPS             Reviewed;         786 AA.
AC   Q0SRU6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=CPR_1847;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM101 / Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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; CP000312; ABG87167.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SRU6; -.
DR   SMR; Q0SRU6; -.
DR   EnsemblBacteria; ABG87167; ABG87167; CPR_1847.
DR   KEGG; cpr:CPR_1847; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000001824; 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_1000093355"
FT   DOMAIN          711..786
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;  88103 MW;  E10FB60DBDE62AC0 CRC64;
     MNDRVLRVLE FNKIKELVKG YAITKSAKEM VLDLKPYDSV YDVKEHLEET KEALDILMRK
     GNPPFEGLYD VKEAITRAEK GGVLSIEGLL RIGNMLSVTR KLSDFLARKE EEEEHRILEG
     MREGLIVLRG VESAISKAIV SEDEIADSAS DKLYSIRRSL KEKNSSIRDK VNSIVRSNAQ
     YLQDSLYTVR GDRYVIPVKA EYKSQVPGLV HDQSSTGATL FIEPTALVNL NNEIKELMLK
     ERAEIERILA ELSALVYKNI DVIKVNFNII VELDFIFAKA KYGSDLGGTM PIVNEEGVID
     LMDARHPLIP KDKVVSSDIY LGREFSTLLI TGPNTGGKTV TLKTTGLIEL MGLSGLLIPA
     SENSSISFFE EIFADIGDEQ SIEQSLSTFS SHMTNIVKIM EKANNKSFVL FDELGAGTDP
     TEGAALAISI LENLRARGCR IMSTTHYSEL KGYALKTENV ENASVEFNVE TLRPTYRLLI
     GVPGKSNAFE ISRRLGLKDN IIEEAKKVIS TESLQFEDLI QSLQEKSIKA ENDAREAAIL
     RNDAEKYKNR YKEKFERIES VRDNVYADAR REAKQILDSA KEEADTILKN MRDLERMGIS
     SDARRKLEAE RGKLRDKISD AEARLQKKKE EQKGEELKKI EVGMEALLPS INQKVIVLSK
     PDNKGEVQVQ AGIMKINVKA KDLRVAKETK EEKKIKKREA RLNLRQVDPS IDLRGMDSEE
     ACYTADKYLD DAYVAGRGEV TLVHGKGTGV LRKAINDMLK KHPHVKSHRL GEYGEGGTGV
     TVVILK
 
 
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