ID A0A3P2AN44_9FIRM Unreviewed; 794 AA.
AC A0A3P2AN44;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=EII17_05565 {ECO:0000313|EMBL:RRD95023.1};
OS Clostridiales bacterium COT073_COT-073.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=2491044 {ECO:0000313|EMBL:RRD95023.1, ECO:0000313|Proteomes:UP000266937};
RN [1] {ECO:0000313|EMBL:RRD95023.1, ECO:0000313|Proteomes:UP000266937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT073_COT-073 {ECO:0000313|EMBL:RRD95023.1,
RC ECO:0000313|Proteomes:UP000266937};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-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:RRD95023.1}.
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DR EMBL; RQYD01000009; RRD95023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P2AN44; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000266937; 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; cd03280; ABC_MutS2; 1.
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 NCBIfam; TIGR01069; mutS2; 1.
DR PANTHER; PTHR48378; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR48378:SF2; SMR DOMAIN-CONTAINING PROTEIN; 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; PS00486; DNA_MISMATCH_REPAIR_2; 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:UP000266937}.
FT DOMAIN 718..793
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT COILED 522..634
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 334..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 794 AA; 87506 MW; DCA397DBDC16F549 CRC64;
MNAKTLKILE YKKITDKLAN YAISPSGRDM ALALLPSTDV TTIRLAQKHT AEAVSLSLKQ
GRLSLRGFHD IRPALKRLPI GSILSMKELL DIADFLMAVE KAIAYFKDLE ELGETLAMAE
FFHQLQSLRN LEREIHRCII SEEEMADDAS PKLADIRRSI KSNQASVKGE LNKLLQSTTV
QGYLQDNIIT IRNNRYCLPV RSEYRNEMPG MIHDQSSSGS TLFVEPMAVI NLNNKLNQLL
LEEEEEIERI LSALSAAAAL DYDALTANLE ALTHLDFIFA KGELALLMDA GQPNFNEDGI
IYLKNARHPL LPAESVVAST IYLGEHFTTL VITGPNTGGK TVSLKTLGLL SLMGQAGLHI
PAADGSQLTV LENIYADIGD EQSIEQSLST FSSHMVNIVE ILKSADYRSL VLFDELGAGT
DPVEGAALAM AILDHLKSRG VLTAATTHYS ELKVYALSTD GVENASCEFD VNTLKPTYRL
LIGIPGKSNA FAISKRLGLS AEIIASAQEF ISGREVRFED LITDLEMNRK TVLLEKERAE
KLHAEVAELN EELRQQKEKL HSQKTEILKQ AKQEAYRILD NAKTEADQII RKMNKIAKSG
DAVKELETER GHLRDKMNAA LSAAEAEKEK SKRQTKIDLK SLKVGQSYLV NSFGQVGTLL
TLPDSGRKVT VQLGIMTATV DVAELRIAAQ TQAPVQAKLK SSYKGSHTAK SMTVSREIDL
RGYNGLDGIE AVDKYIDDVF LSSLNELHII HGKGTGALRS QLHQFLKNDQ RVKSYRLGEI
NEGGAGVTVV TLRK
//
