ID   MUTS2_HALOH             Reviewed;         791 AA.
AC   B8D298;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Hore_05680;
OS   Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC   Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halothermothrix.
OX   NCBI_TaxID=373903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 168 / OCM 544 / DSM 9562;
RX   PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA   Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA   Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT   "Genome analysis of the anaerobic thermohalophilic bacterium
RT   Halothermothrix orenii.";
RL   PLoS ONE 4:E4192-E4192(2009).
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; CP001098; ACL69325.1; -; Genomic_DNA.
DR   RefSeq; WP_012635513.1; NC_011899.1.
DR   AlphaFoldDB; B8D298; -.
DR   SMR; B8D298; -.
DR   STRING; 373903.Hore_05680; -.
DR   EnsemblBacteria; ACL69325; ACL69325; Hore_05680.
DR   KEGG; hor:Hore_05680; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000000719; 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..791
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000118563"
FT   DOMAIN          715..790
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         339..346
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   791 AA;  89692 MW;  D8AE5C9CFB761553 CRC64;
     MEESSLEILE FDKIIDRVQE FAATIIGKEI ISRLQPVDNL NYVKNKLREV SSAREILEEY
     GRPPFGGIRD LREIIEKADK GIVLSVKEVM DVRSTLEGVR ELKKYSREIG TGIDDELQDI
     YSIITEKFDR LTPLKQLENE INRCIDEHGE IKDSASRKLR SIRREMDRIE GKINDKLNSI
     INNTRYQEML QDKLVTIRGN RYVVPVKSSY KNTFSGIVHD QSTSGLTYFM EPMAIVKLNN
     RLGELKRAEE QEIYRILKKL SENIKEHTRD LSDNLEMVSL LDVDFARARF SIEIEGIEPG
     INDKGFINIR GGRHPLLKVK PVPIDITVGN EFKTLVITGP NTGGKTVALK TVGLFVLMVQ
     AGLHIPAEEE TVISIFNGVY ADIGDEQSIE QNLSTFSSHI NRIKRFLGKA DARSLVLLDE
     IGVGTDPREG AALGVAILEH LRERGVTTIA TTHYSEIKSY AYSQDGVENA SVEFDMETLQ
     PTYRLLMGIP GGSNAFEIAL KLGLPHDIIK DGKELMSGDD IKVENIISDL NEERKKYEQL
     KIEIEERLEA VKKKEQKYDS LLTDLEKRKK KLITEAREEA LQIIKKTRKE SKEILRRLKN
     KEFASRSDID RVENEINLNL KETEKEISEK RQNKDGRTRV KEISCGDQVR LKKTGQKGEV
     ISVDREKGEA VIQAGIMKVT TGLDEVAKID IPDDTKDELF HSYQVKKKSR VSPTLDLRGE
     RYETAQHKLD KYLDDVFLAG LKQVEIIHGK GTGALRKAVH TVLEKNPHIT SYRLGRQEEG
     GSGVTIADLK S