ID   MUTS2_SOLM1             Reviewed;         773 AA.
AC   C4XS37;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-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=DMR_20680;
OS   Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS   (Desulfovibrio magneticus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Solidesulfovibrio.
OX   NCBI_TaxID=573370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX   PubMed=19675025; DOI=10.1101/gr.088906.108;
RA   Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA   Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA   Matsunaga T.;
RT   "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT   common gene clusters in magnetotactic bacteria.";
RL   Genome Res. 19:1801-1808(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; AP010904; BAH75559.1; -; Genomic_DNA.
DR   RefSeq; WP_015860746.1; NC_012796.1.
DR   AlphaFoldDB; C4XS37; -.
DR   SMR; C4XS37; -.
DR   STRING; 573370.DMR_20680; -.
DR   PRIDE; C4XS37; -.
DR   EnsemblBacteria; BAH75559; BAH75559; DMR_20680.
DR   KEGG; dma:DMR_20680; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_7; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000009071; 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   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..773
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000202678"
FT   DOMAIN          698..773
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   773 AA;  83749 MW;  4916E7D12EB0E757 CRC64;
     MESRTLSLLE FPKVLDRLAG YAASEPAAAA CRALGPMGDA ARLATEQRKL VEALELRRDR
     AFEFTAFPDI EPLFAVLESE RRVLDLDALV ALSHVLSRVA ALREALGREE GDSVLGAIVY
     RTPWAKKTQA ALARCLGPDG RLKDESSPEL FSVRQEIRSI HQTILTKVKE FISERELGPL
     LQDDYVTISS DRYVLPLRAN FKGRLPGVIH DYSQTGETIY VEPFFLVEIN NRLQELKNEE
     REAEARVMAF LTGLARDERR EVAASYRLLV DCDVLWAKAA LCDAFGGTLP EVAQGRAVRL
     LAARHPLLAL AGPDSAVAQD LELAPDQRAL IVTGANAGGK TVCLKTLGLL AAMALSGLPV
     PAGEGSSLPF FAKIFVFLGD EQSLEDHLST FTAQIRHLSR VWPDIDADTL VLLDEFGAGT
     DPSQGAALAQ AVVDGLLDRG AYLAAATHFP ALKAYGLSRE GVRAACMLFD PATKKPLYRL
     AYDQVGASIA LDVAREHGLP EDILERANRY LLLDGNDTGL VFDRLNDLAL RREHELEAIA
     AKRLAEEGKI QKLKDNLKKA QDKLVEEIRE LSRDIVRRHE AGRLGRKEAQ KALADVRKRL
     IDESNELTGG PGGEAAAVAF DLSVVAPGDS VQVTSWNKIG VVREKDLKRQ AAKVDIGGVS
     LWVNVADLAP AAGKPAKAGG GAVVTPTASE AKGLGLVVDL RGMRADVAES ELLAFVDNAL
     LRGHGELEVI HGRGTGALRR EVHRMLKDHP QVASFAIAPE DRGGDGMTMV TLK