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Database: UniProt
Entry: A0A0V8QGK9_9FIRM
LinkDB: A0A0V8QGK9_9FIRM
Original site: A0A0V8QGK9_9FIRM 
ID   A0A0V8QGK9_9FIRM        Unreviewed;       793 AA.
AC   A0A0V8QGK9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=ASU35_01400 {ECO:0000313|EMBL:KSV59684.1};
OS   Acetivibrio ethanolgignens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=290052 {ECO:0000313|EMBL:KSV59684.1, ECO:0000313|Proteomes:UP000054874};
RN   [1] {ECO:0000313|EMBL:KSV59684.1, ECO:0000313|Proteomes:UP000054874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACET-33324 {ECO:0000313|EMBL:KSV59684.1,
RC   ECO:0000313|Proteomes:UP000054874};
RA   Zou Y., Xue W., Luo G., Lv M.;
RT   "Butyribacter intestini gen. nov., sp. nov., a butyric acid-producing
RT   bacterium of the family Lachnospiraceae isolated from the human faeces.";
RL   Submitted (NOV-2015) 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:KSV59684.1}.
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DR   EMBL; LNAM01000112; KSV59684.1; -; Genomic_DNA.
DR   RefSeq; WP_058352214.1; NZ_LNAM01000112.1.
DR   AlphaFoldDB; A0A0V8QGK9; -.
DR   STRING; 290052.ASU35_01400; -.
DR   OrthoDB; 9808166at2; -.
DR   Proteomes; UP000054874; 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}; Reference proteome {ECO:0000313|Proteomes:UP000054874}.
FT   DOMAIN          718..793
FT                   /note="Smr"
FT                   /evidence="ECO:0000259|PROSITE:PS50828"
FT   COILED          235..266
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          527..625
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         336..343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   793 AA;  88876 MW;  3AE0D7889594577B CRC64;
     MNEKALKTLE YNKIIDKLVA FAGSELGRER CKKLLPMTDI GEIRRNQQET SDALTRVLRK
     GSLSFSGLRD IRASIMRLEV GGVLGMGELL QVSSVLNVAL RVKSYGRSEG SEEETAIDSL
     RERFSLLEPL SPLNNEIKRC ILSEEEMSDD ASPTLRHIRR SIKLTNDRVR EQLNTIVNAS
     SNQTMLQENI VTMRNGRYCL PIKAEYKSQF NGMVHDQSSS GSTLFIEPMA VVKLNNELRE
     LAVKENDEIE RILAELSNQA GEYCQELKDD ITILAELDFI FAKASLSKGM RASEPVFNDK
     GYINIKKGRH PLIDNKKVVP IDIHMGKDFN LLIVTGPNTG GKTVSLKTVG LFTLMGQAGL
     HIPAFDGSEL GVFEEVYADI GDEQSIEQSL STFSSHMVNT VSIIKEANYR SLVLFDELGA
     GTDPTEGAAL AMSILSYLHK KQIRTMATTH YSELKIFALS TEGVENACCE FDVETLRPTY
     RLLIGIPGKS NAFAISSKLG LPDYIITDAK ERIGEKEQSF EDVISDLEKS RVTMEKDQEE
     IARYKEEVER LKKKLEQKNE RIDEAKEKIL RRANEEAREI IQEAKDFADE SIRKYNKWMK
     DGSMNREMEK QRSELRDKLN STESKLALKG QKAKKQHKAS DFKIGDAVRV LSMNLNGTVS
     SLPNDKGDLF VQMGILRSQV NIKDLELIDE PVITGPNMKK TGSGQIKMAK TAYISPELNL
     IGKLVDEALP ILDKYLDDAY LAHLPQVTII HGRGTGALRN AVHNHLKKTR YVKSYRVGGF
     GEGDHGVTIV EFK
//
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