ID A0A1C2GJ00_9SPHI Unreviewed; 784 AA.
AC A0A1C2GJ00;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BEL04_15865 {ECO:0000313|EMBL:OCX51500.1};
OS Mucilaginibacter sp. PPCGB 2223.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1886027 {ECO:0000313|EMBL:OCX51500.1, ECO:0000313|Proteomes:UP000095113};
RN [1] {ECO:0000313|EMBL:OCX51500.1, ECO:0000313|Proteomes:UP000095113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PPCGB 2223 {ECO:0000313|EMBL:OCX51500.1,
RC ECO:0000313|Proteomes:UP000095113};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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:OCX51500.1}.
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DR EMBL; MDJS01000003; OCX51500.1; -; Genomic_DNA.
DR RefSeq; WP_066005768.1; NZ_MDJS01000003.1.
DR AlphaFoldDB; A0A1C2GJ00; -.
DR STRING; 1886027.BEL04_15865; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000095113; 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:UP000095113}.
FT DOMAIN 709..784
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT COILED 529..627
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 341..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 784 AA; 88900 MW; FE80438E775FCB1B CRC64;
MLYPNNSVDK LGFTEVKELI KTHCLSIMGQ QMVDRIQVMS NYDQIRKFLS QAQEFKNILQ
NDSPLPIHHF FDIKSLANKA RLEGAFLTEE EFFQIQASLT TVFAVISYFN EREGRYPDLE
ALFEHLPIER TILKQIDRVI DQKGKIRPNA SAELMEITSG IARAEQEARR KIDQIFKNAT
SNGWTADGSL TVRDGRLCIP LLAENKRKLK GFIHDESASG QTVYMEPDEV FSLNNKIRDL
EFERRREIVK ILTALTDELR PHTPLLLSYH SLLTKLDFVR AKALFAIDIE AQMPVLHNDA
RIKLVNARHP LLFLSFKKEH KTVVPLNVQI DEQDRIIVVS GPNAGGKSVC MKTVGLLQMM
VQAGLLIPAH ETSEAGVFKQ LFVDIGDDQS IESDLSTYSA HLSKMKHFVE QANGKTLILI
DEFGTGTDPQ FGGPIAEAVL ESLNHKKVKG MVTTHYSNLK IFASNTAGLQ NASMLFDNKE
MRPLYMLEVG KPGSSYAFEI AQKIGLPKEV LSLAKNKIGD SQKKVDTLLI DLEREKNELY
LARVQLEKQQ RRANELLREN EKQKAYYEEN KRTLVSEAKQ EAKNIILNAN KLVENTISEI
KSSNADKEKT RELREKLNNE VKKNTVKPIA PKPTAEELKV GDWVKLNDSD TTGVIMEIAR
DNLIIAIGDL RTVAKKNRVQ KVSKKEVPKE VRRSYSGDTG SLANFSPEID VRGKRGEEAL
YEIEKYLDKA IMMGFGNLKI IHGKGDGILR KLIRDYLRKY SEVDRMEDEH ADRGGDGITY
VYLK
//
