ID A0A374W5Q4_9BACE Unreviewed; 832 AA.
AC A0A374W5Q4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=DXB63_16370 {ECO:0000313|EMBL:RGN42834.1};
OS Bacteroides sp. OM05-12.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=2292283 {ECO:0000313|EMBL:RGN42834.1, ECO:0000313|Proteomes:UP000264777};
RN [1] {ECO:0000313|EMBL:RGN42834.1, ECO:0000313|Proteomes:UP000264777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM05-12 {ECO:0000313|EMBL:RGN42834.1,
RC ECO:0000313|Proteomes:UP000264777};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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:RGN42834.1}.
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DR EMBL; QSUN01000033; RGN42834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A374W5Q4; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000264777; 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; 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:UP000264777}.
FT DOMAIN 757..832
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT REGION 649..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 346..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 832 AA; 94588 MW; 5B7B9B1A05CC3700 CRC64;
MIYPHNFEQK IGFDDIRRLL KEKCLSSLGE GRVDEMNFSD SFNEIEERLN QTNEFVRIIQ
EEDSFPAQYF FDVRPSLKRI RVEGMYLDEQ ELFDLRRSLE TIRDIIRFLS SEDEEENSPY
PNLKKLAGDI AVFPQLITRI NGILNQYGKI KDNASQDLLR IRRELASTTS GISRSLNAIL
RSAQSEGYVD KDVAPTMRDG RLVIPVAPGL KRKIKGIVHD ESSSGKTVFI EPAEVVEANN
RIRELEGEER REIIRILTSF SDTLRPSVPD ILQSYEFLAE VDFIRAKAYF ALQTNSLKPA
LESEPLIDWT MAIHPLLQMS LAKHGKKVVP LDIELNSKQR ILIISGPNAG GKSVCLKTVG
LLQYMLQCGL LIPLHERSHA GIFGSIFIDI GDEQSIEDDL STYSSHLTNM KIMMKSCDER
SIILIDEFGG GTEPQIGGAI AEAVLKRFNH KKTFGVITTH YQNLKHFAED HEGVVNGAML
YDRHLMQALF QLQIGNPGSS FAVEIARKIG LPEDVIADAS AIVGSEYINA DKYLQDIVRD
KRYWEGKRQT IRQREKHMEE VIAKYEADIQ ELDKSRKEII RKAKEDAERL LQESNAKIEN
TIRTIKEAQA EKEKTRIARQ ELNEFRESME DIEKKNTEEK IARRMEKLRE KQNRKKERKD
KSQEVQSKPQ TPKTESIEIG CQVKMKGQSS IGDVLEINGK NVVVAFGMIK TTVKLDRLER
VKPSNSQPKN TNTKSTFVSS QTQDSVYEKK LGFKQDIDVR GMRGDEAIQA VTYFIDDAIL
LGIDRVRILH GTGTGILRTL IRDYLKTVPG IAHFQDEHVQ FGGAGITVVD LS
//
