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Database: UniProt
Entry: A0A3M8ECS7_9BACT
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ID   A0A3M8ECS7_9BACT        Unreviewed;       808 AA.
AC   A0A3M8ECS7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=D7D25_13775 {ECO:0000313|EMBL:RNC63909.1};
OS   Proteiniphilum sp. X52.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC   Proteiniphilum.
OX   NCBI_TaxID=2382159 {ECO:0000313|EMBL:RNC63909.1, ECO:0000313|Proteomes:UP000272792};
RN   [1] {ECO:0000313|EMBL:RNC63909.1, ECO:0000313|Proteomes:UP000272792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X52 {ECO:0000313|EMBL:RNC63909.1,
RC   ECO:0000313|Proteomes:UP000272792};
RA   Hivarkar S., Lanjekar V.B., Dhakephalkar P.K., Dagar S.;
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:RNC63909.1}.
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DR   EMBL; RDSD01000020; RNC63909.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8ECS7; -.
DR   OrthoDB; 9808166at2; -.
DR   Proteomes; UP000272792; 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; cd06503; ATP-synt_Fo_b; 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}.
FT   DOMAIN          733..808
FT                   /note="Smr"
FT                   /evidence="ECO:0000259|PROSITE:PS50828"
FT   REGION          625..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          533..610
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         345..352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   808 AA;  91868 MW;  4322AD283D42B34F CRC64;
     MIYPDNFEQK IEFQKVRQLL SERCLSPLGK EKVEEMHFSA SYGEIEPLLF QTEEFVRIGE
     EEDSFPADHF YDMRPVLRRI RVEGAWIDQN ALFELRRSLQ TIHGIVAFLR RDEGKAPKYP
     YLLALAGGIP TFPEMTRRID SILDGFGQVK DHASPRLSEI RRELTSTLNG ISKSLNAILR
     KAQAEGYVDK DVSPSMRDGR LVIPVNPSHK RKIKGIVHDE SASGKTVFIE PSEVVEANNR
     IRELEADERR EIIKILTDFT NYLRPSLPDL LESYEFLAKI DFIQAKAAFA RLIGGIKPSI
     DNTPRIDWVE AVHPLLYLSL KKQNRKIVPL DIILEGDNRL LVISGPNAGG KSVCLKTVGL
     LQYMVQCGLL IPLKENSRVG VFDDIFIDIG DEQSIENDLS TYSSHLLNMK FFEKHCNDKS
     LLLIDEFGSG TEPRIGAAIA EALLDRFNRR QSFGVITTHY QNLKHFANEN EGVVNGAMLY
     DRHEMQPLFR LAIGNPGSSF AVEIARKTGI PEDVIAHASE IVGKDYIDMD KYLQDISRDK
     RYWERKRDEI RRERKRLEEI TSKYEADLET IHKQKKEILA QAREQAERLL AESNARIENT
     IREIREAGAD KEKTKQIRQS LREFKEKMEP VDMPETKKRK KQKQRRTAGD DNGLKAAQPL
     AAGDTVRLIG QSSPGEIMEI SGKKAVVAFG MIKSTVDLDK LERVSANQIK KERKVSNTRD
     LLHERKLNFK QDIDVRGMRG DEALQAVMYF VDDAIQLGVS RVRILHGTGT GALRQVIREY
     LGSVHGVARF QDEHVQFGGA GITVVDLE
//
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