ID A0A399SGI3_9BACT Unreviewed; 798 AA.
AC A0A399SGI3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=D1627_07955 {ECO:0000313|EMBL:RIJ41929.1};
OS Pontibacter oryzae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=2304593 {ECO:0000313|EMBL:RIJ41929.1, ECO:0000313|Proteomes:UP000266005};
RN [1] {ECO:0000313|Proteomes:UP000266005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIRAN {ECO:0000313|Proteomes:UP000266005};
RA Seo T.;
RT "Mucilaginibacter sp. MYSH2.";
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:RIJ41929.1}.
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DR EMBL; QWGE01000002; RIJ41929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399SGI3; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000266005; 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; SSF47857; Apolipophorin-III; 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}.
FT DOMAIN 723..798
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT REGION 691..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 524..561
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 588..615
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 343..350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 798 AA; 89832 MW; CC6EC5DDA179EA27 CRC64;
MIYPENFEIK IGFAQVREML SELCLSPLGR HFVSRMQFLN RHDLLERLLQ QTEEFKQLLE
SDAEIPLQHY YDPTAYLDRA ALEGTFLDVV QFFEIKMSLR TIRDSLRFIS ESEEGKYEAL
KALGANVAVE RSLLAALDKV VDDTGAVRDD ATPELQRLKR DLIAQQAALR KTISSILRHA
KNEGWTPSDV EPTIRGGRLV IPVIAEHKRR IKGLIHDESN TGQTVYIEPE SIFELNNDIK
DLENAYHREL IRILVGLTNT LRHHIPELRK AYQYLGLLDF IRAKAVFARR VESTKPTLHK
YPLINWKQAF HPLLYLAHKQ AGKPVVPMDL ELNRDQRLLL ISGPNAGGKS VSLKTVGLVQ
YMLQCGLLIP AADNSEAGVF HDIFIDIGDE QSIENDLSTY SSHLTNMKKF VTVADKRSLV
LIDEFGTGTE PVLGGAIAEA VLQNLNESSV YGVITTHYTN LKNYAERTPG IVNGAMRYDH
KHLQPLYQLE IGKPGSSFAI EIAQKIGLPK HIIDRASKLV GKDKIRYDRL LEELETEKQE
LEKKVREASK LEQKLTKSVK EYGDLRNFLE ESKQDVMREA KGKAKLLLKD ANQKIEATIQ
QIKQSQAEKE KTKEARRDLE TFAQEVRKDE PRPAHKRIAN GSVKPGDNVA LIGQDSVGQV
VSIKGKTAEV LFGGLKTIVK VDNLERIEGQ VSQKPKKSKM ENAGGFSRGM NMTQRMSDFT
STLDIRGEYA EDALTKVMNF TDEALMLGIP EIKIIHGRGN GVLRQVVRDY LYSVREVASV
GNEAEERGGD GATLAVLK
//