MUTS2_ACET2
ID MUTS2_ACET2 Reviewed; 793 AA.
AC A3DE67;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Endonuclease MutS2 {ECO:0000255|HAMAP-Rule:MF_00092};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00092};
GN Name=mutS2 {ECO:0000255|HAMAP-Rule:MF_00092}; OrderedLocusNames=Cthe_1014;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) 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:0000255|HAMAP-
CC Rule:MF_00092}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00092}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00092}.
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DR EMBL; CP000568; ABN52246.1; -; Genomic_DNA.
DR RefSeq; WP_004463478.1; NC_009012.1.
DR AlphaFoldDB; A3DE67; -.
DR SMR; A3DE67; -.
DR STRING; 203119.Cthe_1014; -.
DR EnsemblBacteria; ABN52246; ABN52246; Cthe_1014.
DR KEGG; cth:Cthe_1014; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000002145; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor 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 Gene3D; 3.30.1370.110; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002625; Smr_dom.
DR InterPro; IPR036063; Smr_dom_sf.
DR PANTHER; PTHR11361; PTHR11361; 1.
DR PANTHER; PTHR11361:SF14; PTHR11361:SF14; 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; SSF160443; SSF160443; 1.
DR SUPFAM; SSF48334; SSF48334; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01069; mutS2; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR PROSITE; PS50828; SMR; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..793
FT /note="Endonuclease MutS2"
FT /id="PRO_1000093356"
FT DOMAIN 718..793
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 335..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 793 AA; 88690 MW; 5B0DCC0B54BF7D63 CRC64;
MNEKTLKILE FNKIIDKLVS LATSSLGKEL AEKLVPDTDL NRVERAQKET SDAVAFIARR
GTPPMGGIHD IRDSLKRVEI GAILNPGELL KTADVLRAVR NLKSYASNDR IKTDEDNIVS
ELIGCLESNK RIEDRIYMSI LSEDEIADNA SPTLANIRRQ IRNAQESIKD KLNDIIRSSR
YQKYIQEPIV TLRGDRYVIP VKQEYRTEIP GLIHDSSASG ATIFIEPMAV VEANNHIREL
KIKEQAEIEK ILGELTGEIR GIVDSLKSNV SILGRLDFIF AKARLSLDYN CVCPVLNDEH
KILIKKGRHP LLDKKTVVPI DFWIGEDFNT LVVTGPNTGG KTVTLKTVGL FTLMTQAGLH
IPANEGTKMS IFKKVYADIG DEQSIEQSLS TFSSHMKNIV GILKDVDEDS LVLFDELGAG
TDPTEGAALA MSILEYLRNK GSTTVATTHY SQLKAYAVTT KFVENACCEF NVETLRPTYR
LLIGVPGKSN AFAISKRLGL FDDIIEKAKE FLTQDDIKFE DMLMSIEKNL NQSENEKMKA
ESYRLEAEKL KKELEEQKRK LAENRERLIQ EARAEARKIL LEARKEAEEI ISKMRRLEQE
VHNAQRQKEA EELRLKLKRK VDSIEETLEL PLAPKNALVK PPENLKPGDS VLIVNLDQKG
TVITPPDKDG EVVVQAGIMK INVHISNLKL VDEQKIVLNN SGIGKIGMSK AKSISTEIDV
RGYNLEEAIE SVDKYLDDAY LSGLTEVSII HGKGTGVLRS GIQKFLKSDS RVKSFRLGKY
GEGESGVTIV ELR