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Database: UniProt
Entry: R5SNU1_9FIRM
LinkDB: R5SNU1_9FIRM
Original site: R5SNU1_9FIRM 
ID   R5SNU1_9FIRM            Unreviewed;       783 AA.
AC   R5SNU1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=BN540_00870 {ECO:0000313|EMBL:CCZ54833.1};
OS   Dialister invisus CAG:218.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Dialister.
OX   NCBI_TaxID=1263072 {ECO:0000313|EMBL:CCZ54833.1, ECO:0000313|Proteomes:UP000017966};
RN   [1] {ECO:0000313|EMBL:CCZ54833.1, ECO:0000313|Proteomes:UP000017966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:218 {ECO:0000313|Proteomes:UP000017966};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ54833.1}.
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DR   EMBL; CBAF010000115; CCZ54833.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5SNU1; -.
DR   Proteomes; UP000017966; 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   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; 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; 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; 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:UP000017966}.
FT   DOMAIN          708..783
FT                   /note="Smr"
FT                   /evidence="ECO:0000259|PROSITE:PS50828"
FT   COILED          515..559
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         333..340
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   783 AA;  88228 MW;  5F68BFFCC474752F CRC64;
     MEQDILQILE FNEIRRMLAQ LCPSSLSKAK AIDLQPSSEP RIIAEHLQET EEASICLQKE
     ISSPLGETYD IIPFIDRAEK EMILLAGEFM EISSSLETYQ KMHEYFSGER HLRYPILEEK
     ASLILPLDGL LNRIRQVFDD KGDIRDKASM KLSRIRGDIE TVKSRIRKSF RQILHDKDTT
     LYLQDAIITQ RNGRYVVPVK EEYRYKFDGI VHDRSSTGQT LFMEPMISVR LNNDLIELVL
     AEKQEVMEVL RELTRQIKNN SAVIRKDCHI VSDMEFIFAR GQLALAMNGV RATFSAAGIL
     DLKDARHPLI PADRVVPISL TLGKAFKILV ITGSNAGGKT IAIKTVGILA LMNQSGLFIP
     AAEGSMMPVY NHIYSIIGDD QSIQYNLSTF SSYITQLVSF LPYVNEKDLV LLDELGAGTD
     PIEGAMLAQA VTEYLVNKNV NSIITSHFSE MKKLAYELSE VENAFVEFDK ETLSPTYHLI
     IGVAGNSNAF NICRRLGMQE SILNRAVELQ QRSPFHNMEM VMNHLNEQRK ELEQEKESIR
     IIRQESDGVR AQLQEEQEEF LLKKNAILSK MREESSDIKR NLRIQAEKII RDVKKASSLD
     KDAFMKHVGT TRSAIENMKI PESRSKRGLV ANEIKRGDII YIDTLGSNGK VISVTGKKIT
     VACGVANICV DISHCFAAEQ LVKMIPQKIS HQKKNVSNLR HEEVSTSVNV IGKTVYEAIP
     EIDKFLNDCI MAGVSPVQII HGKGTGSLRK GIHDYLKTLP FITDFRMAEP QNGGAGVTDV
     YFN
//
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