ID A0A0A2DLU2_9PORP Unreviewed; 867 AA.
AC A0A0A2DLU2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=HQ37_07900 {ECO:0000313|EMBL:KGN67556.1};
OS Porphyromonas sp. COT-239 OH1446.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1515613 {ECO:0000313|EMBL:KGN67556.1, ECO:0000313|Proteomes:UP000030150};
RN [1] {ECO:0000313|EMBL:KGN67556.1, ECO:0000313|Proteomes:UP000030150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-239 OH1446 {ECO:0000313|Proteomes:UP000030150};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas sp. COT-239_OH1446 Genome sequencing.";
RL Submitted (AUG-2014) 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:KGN67556.1}.
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DR EMBL; JRAO01000035; KGN67556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2DLU2; -.
DR STRING; 1515613.HQ37_07900; -.
DR eggNOG; COG1193; Bacteria.
DR Proteomes; UP000030150; 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 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; PS50828; SMR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00092};
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:UP000030150}.
FT DOMAIN 792..867
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT REGION 639..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 358..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 867 AA; 98169 MW; B0A987191796C871 CRC64;
MGRVAHYPES FEAKIAFDEV RMLVAEHALT PMGRERVEGL VCRDDFSTLS QELTQVQEMQ
QLLRGELELP SLRVVDCREA LQRIRPQGTY IEQEELADLL QMLRSLHALY YFFRVQTASG
SVEDESLTFL YPELSRVLEN CPTFPKIEQA MARLLGKDGK IRDNATGELL RIRTELSDTE
RSISGSLQRI LRTARAEGWV EEGVQPSLRD GRLVIPVSPM YKRKIKGIVH DESATGRTVY
IEPVELVEAN NRIRELEAEE RRELIHILTE IANKLRPNLS HLLGAYELLG VIDFIRSKAQ
WGLSHEAICP RLEAEPRLEW FGAKHPLLMR SLKAQGREIV PLDIELSLPE RRLLIISGPN
AGGKSVCLKT VGLLQYMVQC ALPIPVAEQS RVGVFSRLFI DIGDEQSIED DLSTYSSHLS
NMKHFARECD PETLILIDEF GGGTEPTIGG AIAQALLHRF NEQGAWGVIT THYQNLKTFA
EDHEGLVNGA MLYDRHEMRP LFRLSIGRPG SSFAIEIARK IGLPEEVIQE ARQIVGSDYI
DMDKYLQDII RDKRYWEGKR ESIRREEKAL QQAAQKYHDE IAALKAQRAE LLAEARDEAK
RIVNEAGSRV ERTIREIKEA EAERERTISL RQELRSYQED LSTETEDDGL SAQKAQREVE
RILRRRERKA GRGQGSKDEA KVVAKLRQLT QQAAQGPEAS AEQRPQWTVG QEVRIEGQQS
VGTILSIKDE EAIVAMGMLK VTIALDRLRQ PNGKDKSQTK QQQKAQSLTL GQRHSSILDQ
LREKRLHFKQ DLDLRGMRVN EALEATTYFV DDALQLGISR VRILHGTGTG ALREAIRQYL
SGVPGVRHYA DEHVQLGGAG ITVIDLE
//
