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Database: UniProt
Entry: A0A2S6FXY1_9CLOT
LinkDB: A0A2S6FXY1_9CLOT
Original site: A0A2S6FXY1_9CLOT 
ID   A0A2S6FXY1_9CLOT        Unreviewed;       786 AA.
AC   A0A2S6FXY1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Endonuclease MutS2 {ECO:0000256|HAMAP-Rule:MF_00092};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00092};
GN   Name=mutS2 {ECO:0000256|HAMAP-Rule:MF_00092};
GN   ORFNames=BD821_10795 {ECO:0000313|EMBL:PPK48458.1};
OS   Clostridium algidicarnis DSM 15099.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121295 {ECO:0000313|EMBL:PPK48458.1, ECO:0000313|Proteomes:UP000239863};
RN   [1] {ECO:0000313|EMBL:PPK48458.1, ECO:0000313|Proteomes:UP000239863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15099 {ECO:0000313|EMBL:PPK48458.1,
RC   ECO:0000313|Proteomes:UP000239863};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_00092}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00092}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00092}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PPK48458.1}.
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DR   EMBL; PTIS01000007; PPK48458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6FXY1; -.
DR   STRING; 37659.GCA_000703125_02337; -.
DR   OrthoDB; 9808166at2; -.
DR   Proteomes; UP000239863; Unassembled WGS sequence.
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; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR48378:SF2; SMR DOMAIN-CONTAINING PROTEIN; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00092}; Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00092};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00092}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00092};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00092};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00092}.
FT   DOMAIN          711..786
FT                   /note="Smr"
FT                   /evidence="ECO:0000259|PROSITE:PS50828"
FT   COILED          523..620
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         332..339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   786 AA;  88331 MW;  5512F24B86651FB0 CRC64;
     MNNRALKILE FSKVKDEIKR YASTKAAKDI IDDLVPYTNV YEVNRSLKET EEALNSMVKK
     GPPPFYGLYD VRDYLIRIEK GGGVLATNLL KIAQMLRCSR GIKDYVNRKV EEESFPMLEN
     ICEGIVPLKY LEEEIFRIIV SDEEISDRAS DTLYTIRRSL KDKNSSLKDK VNSLIKTYSK
     YLQENLYTVR GDRYVIPVKA EHKGMVPGLV HDQSSSGATL FIEPMGLVNL NNDIKELMLK
     EEAEIERILD ELCFKIYEKI EVIKVNAQII WEIDFIFSKA KYASEINAIK PKVNEDGSFN
     IIQGRHPLID PKVVVPSDIY LGKDFTSIVI TGPNTGGKTV TLKTVGLLHV MAMSGVMIPA
     AYNSSINFFD EVFADIGDEQ SIEQSLSTFS SHMTNIVSII KEANKGSLVL LDELGAGTDP
     TEGAALAMSI LEDLKSKDVK IIATTHYSEL KVYAINTKGV ENASVEFDVK TLRPTYRLLI
     GIPGKSNAFE ISRKLGLPDY IIQSSKELIS KDSLEFEDLI ESLQSKSVDA DKFEREARLL
     KEESEKLKEK YEQKLQALET SKEKILEESK RKAKIALKDA KEEADAILKN IRELEKMGYS
     SKARQDIEEH RNKLAKELDK QSTTLIPKEH KGEKLVSVKL GEEVFVPSLN QNVIVLTNPD
     NKGEVQVEAG IMKINLKLED LRKINNNKSS KERRNSKKQV NLNLKSVGAS VDLRGQDSEE
     ACYNADKYLD EAYLGGLGLV SLIHGKGTGV LRKAINDMLK RHPHVKNFRL GEYGEGGDGV
     TMVQLK
//
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