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Database: UniProt
Entry: A0A494XV36_9BACL
LinkDB: A0A494XV36_9BACL
Original site: A0A494XV36_9BACL 
ID   A0A494XV36_9BACL        Unreviewed;       787 AA.
AC   A0A494XV36;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=D7Z26_11170 {ECO:0000313|EMBL:RKP54481.1};
OS   Cohnella endophytica.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2419778 {ECO:0000313|EMBL:RKP54481.1, ECO:0000313|Proteomes:UP000282076};
RN   [1] {ECO:0000313|EMBL:RKP54481.1, ECO:0000313|Proteomes:UP000282076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M2MS4P-1 {ECO:0000313|EMBL:RKP54481.1,
RC   ECO:0000313|Proteomes:UP000282076};
RA   Tuo L.;
RT   "Cohnella sp. M2MS4P-1, whole genome shotgun sequence.";
RL   Submitted (OCT-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:RKP54481.1}.
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DR   EMBL; RBZM01000005; RKP54481.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494XV36; -.
DR   OrthoDB; 9808166at2; -.
DR   Proteomes; UP000282076; 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: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 {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}; Reference proteome {ECO:0000313|Proteomes:UP000282076}.
FT   DOMAIN          712..787
FT                   /note="Smr"
FT                   /evidence="ECO:0000259|PROSITE:PS50828"
FT   COILED          522..599
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         334..341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   787 AA;  86948 MW;  E72278781A0D7D8C CRC64;
     MNDKALHTLE YDKIVQRLIG LTSTSLGREE AEKLSPSREL SVVQRRLAAT DEASRAVALK
     GTAPFGGITD IRSSLYRAKL QGILQPPELM EVAQFIMGSR RLNRFIALAG EETALPLLAD
     LCEPLTDYKA LEDDIRRCID EQGEVLDSAS PELASVRRDI RINAGRAREK LESLVRSSSV
     QKMLQDALIT MRNDRYVIPV KQEYRAHFGG IVHDQSGSGA TLFIEPEAVV QMNNKLRELK
     IKEQNEVERI LRKLTEQVGE RADLLTGDAE LLGMIDFIFA KASLAHALHA TLPEMNDEGK
     LLLHKARHPL IEFKQAVPID IELGETYTSI IVTGPNTGGK TVSLKTIGLL SLMAMSGLFI
     PAEDGSKLCV FDGIYADIGD EQSIEQSLST FSSHMTNLIS MLNQVTRRSL VLLDELGAGT
     DPAEGSALAI AILEHLQKLG CRLIATTHYS ELKAYAYNRE GIINASMEFD VATLRPTYRL
     LVGVPGRSNA FAIAERLGLP KSIIDHARGE VSEDELKVDS MIASLEQDRL QAQSERQLAE
     RMRREVEKLQ SDMEEERFKL QEQKAKLLEN AREEARQAIS KAKREAEEII GDLRRLALEE
     GASVKEHKLI EARRRLEDAV PSPVAKPNRS SGAKQGKIES GDEVKVLSLG GQKGHVVELI
     GGSEAMVQLG ILKMKVALAD LEPMRKSASS KAPIAQATIV KRSRDENVRT ELDLRGMMLD
     EAIMEVDRFL DEAFLSNLGQ VYIIHGKGTG ALRTGVQEFL RRHKHVKSYR LGQFGEGGAG
     VSVAELH
//
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