ID   MUTS2_CARHZ             Reviewed;         777 AA.
AC   Q3ABU1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=CHY_1564;
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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; CP000141; ABB15085.1; -; Genomic_DNA.
DR   RefSeq; WP_011344468.1; NC_007503.1.
DR   AlphaFoldDB; Q3ABU1; -.
DR   SMR; Q3ABU1; -.
DR   STRING; 246194.CHY_1564; -.
DR   PRIDE; Q3ABU1; -.
DR   EnsemblBacteria; ABB15085; ABB15085; CHY_1564.
DR   KEGG; chy:CHY_1564; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000002706; 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   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..777
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093343"
FT   DOMAIN          702..777
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         328..335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   777 AA;  88282 MW;  45CA83670C1EED15 CRC64;
     MNQKTLEKIE FPDIINKLWQ KAESFPGKQL ALKVRPLSDS KIIEEKLLEV EEGLSYLRFK
     TVDLSVLSDF SEIFLKLSKE SMLTGQEIYR LGQLLKVSKD TFFEISRGAF PRLKQIVKLL
     FFDEALVKDI ERSFWPEGTV KDEASPELKR IRGQIARLKD KMREAVEKYL KEPELAKYLQ
     EPLISVRGDR FVLPVKASYK SQVPGIIHDR SNTGQTLFIE PYSAVEAGNE LKTLELQEKE
     IIEKILKDFT QRLACNLTEI KRTYELLGEI DLIVAKARLA LELDAYKPRI SENGVLSFKQ
     ARHPLLGKKA VPFDLTLGKE FDLLIITGPN TGGKTVTLKT IGILTIMARA GLFIPASPET
     EIGLFGEVYV DIGDEQSIVQ SLSTFSSHLL NLKFILENAR EGDLVLLDEL GTGTDPREGA
     ALAKAILEEL RGKKVKVVAT THTSELAAYA IETERVENAS VEFDPESLKP TYRLHIGKPG
     RSNALYIAQG LGLKEQIIEK AKSFLKEEEL KLDKLIFDVE QEKRQLEKAK EEVANLLISL
     KEKEAKLNDE LENLEKTKEE IIRKYREKYQ QKLLEIERKG KLVIEEIKEK IKTYEEKNLA
     KLLEEARQKT KEFSQNFALP FEPIKPYRPK VGETVELVEV GQKAEVLAVG ENYAIVQAGI
     MKLNVSFDQI RPAQKQEKEN EKGQVKKAGL ELTKKQNFNL ELDIRGMNTL EAEPVVEKYL
     DNAYLAGVEK VRIIHGKGTG ALKKFLWDYL REVPFVKKFN FAPQNQGGDG ATEVYLK