ID   MUTS2_AGARV             Reviewed;         792 AA.
AC   C4ZI07;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
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=EUBREC_2915;
OS   Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS   / VPI 0990) (Eubacterium rectale).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Agathobacter.
OX   NCBI_TaxID=515619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC   0990;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(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; CP001107; ACR76644.1; -; Genomic_DNA.
DR   RefSeq; WP_012743671.1; NC_012781.1.
DR   AlphaFoldDB; C4ZI07; -.
DR   SMR; C4ZI07; -.
DR   STRING; 515619.EUBREC_2915; -.
DR   PaxDb; 515619-EUBREC_2915; -.
DR   KEGG; ere:EUBREC_2915; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   Proteomes; UP000001477; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis 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; P-loop containing nucleotide triphosphate hydrolases; 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; IPR046893; MSSS.
DR   InterPro; IPR005747; MutS2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002625; Smr_dom.
DR   InterPro; IPR036063; Smr_dom_sf.
DR   NCBIfam; TIGR01069; mutS2; 1.
DR   PANTHER; PTHR48378:SF1; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48378; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF20297; MSSS; 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; SSF48334; DNA repair protein MutS, domain III; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF160443; SMR domain-like; 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..792
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000202680"
FT   DOMAIN          717..792
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   792 AA;  87574 MW;  4246F3B54A909D71 CRC64;
     MNKKVYKTLE YNKILTMLSS YAACDETKKR CLSLEPITDL YEIRHLQTTT ADALSRLYKD
     SGVSFVGIHN VHASLKRLDI GGALNTTELL RICSLLEVAK RVKAYGRSAM DNEKQDSLSG
     LFAGIEPVSA LCDEIKRCIL SEEEIADDAS PELFKIRKSI RGMNDRIHAQ LTKLMNNSTT
     RTYLQDAVVT MRDGRYCLPV KAEAKGNVPG MMHDQSSTGS TLFIEPMAVV NLNNELKELF
     IKEQEEIEKI LAALSDKVAM NAAALEQDYE ILSELDFIFA KANLAKSYNG VAPDFNTDGH
     INIRKGRHPL LDAKKVVPID VRLGEDYKQL IITGPNTGGK TVSLKTVGLL TLMGQAGLHI
     PAADRSKLAI FEDVFADIGD EQSIEQSLST FSSHMTNIVK ILEKADDRSL CLFDELCSGT
     DPTEGAALAI SILNRLHQYG AITMATTHYS ELKVYALSTD GVENACCEFN VETLSPTYRL
     LIGIPGKSNA FAISSKLGLD ENIIEDAKSR INDNDLDFED LIASLESQRQ TIEKEQLEIN
     SYKAEIEKLK KQLEEKNERI DKSKDKILRE ANEEAYKILQ DAKELADKTI RNFNKYGQGQ
     APMSQMEKER SALRDKMNDK EKKLSDIKKN TAKANHKAPK KLRIGDSVLV LSLNLKGTVH
     TLPNAKGDLY VQMGILRSLV NINDLVLLND DVSPAKKYGG SGSKIKMSKS LSVSSEINLI
     GKTTDEALAL LDKYLDDAYI AHLSSVRIVH GKGTGALRKA VHGLLKRTKT IAEYHLGEFG
     EGDAGVTIAT FK
//