MUTS2_CALS8
ID MUTS2_CALS8 Reviewed; 787 AA.
AC A4XK62;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Csac_1710;
OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS 6331).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX NCBI_TaxID=351627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331;
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 Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA Kengen S.M.W., Richardson P.;
RT "Genome sequence of the thermophilic hydrogen-producing bacterium
RT Caldicellulosiruptor saccharolyticus DSM 8903.";
RL Submitted (APR-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; CP000679; ABP67297.1; -; Genomic_DNA.
DR RefSeq; WP_011917231.1; NC_009437.1.
DR AlphaFoldDB; A4XK62; -.
DR SMR; A4XK62; -.
DR STRING; 351627.Csac_1710; -.
DR EnsemblBacteria; ABP67297; ABP67297; Csac_1710.
DR KEGG; csc:Csac_1710; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000000256; 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.
FT CHAIN 1..787
FT /note="Endonuclease MutS2"
FT /id="PRO_1000093342"
FT DOMAIN 711..786
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 331..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 787 AA; 89592 MW; 010F278CF8593872 CRC64;
MNQKTLKALE YDKIVEILKN MAKSTPAKEY FENLIPSTNL ADIENELNKV DEGYRYVLKY
GNPPTLEFEN ILPSLKKSKL GATLNPHEIL QIGKVLKLSY EMRSYLSYTQ DFSFLESMKK
RLVNLKEVIS RIDQTFLTAD EILDTASPRL KEIRDRIRKL ESRIRDELNS MIRDPKIQRF
LQEPIITIRG EKLLLPVKAE FRNEVKGIVH DQSATGATLF VEPFVCVEIS NQIRILKSQE
KEEIERILQE ISSLIASYCD EIETSFYALV ELDIVFTKAI WAKEMNASKP VINTSGIINL
KKARHPLIQK DKVVPIDIHL GKDFDVLIIT GPNTGGKTVT LKTVGLFCLL CQSGIFIPAD
EDSQLCIFQK IFADIGDDQS IVQSLSTFSA HMKNIIEITK NADDKTLVLL DEIGAGTDPE
EGAALAKAIL KYLSEKGSKV IATTHYGELK IFAQQEDRFE NASCEFDVKT LKPTYRLLIG
IPGRSNALVI SSNLGLDKGI VEMARGYLSQ KTIDLDRIIN EMEQKRKEAE ENLELARKLK
LEAQALKAAY EEEKKRFETE RERIRKKAIN EAKEIVERAQ YEIENLFKDL RKLAENLKEK
EVLKELEEKK REYERLIQSI SQQEKQEAES KTKKTLQNIR LGQKVYVRSF DAVGFVESLP
DSKGNLTVQI GIMKLNVNIS DIEEVEEGEK KVYQTTSKNV KLREKSVDLS IDVRGKTSDD
AILDVDKYLD DAYTSGLRQV TIIHGKGTGV LRQAIRNFLK RHPLVKSFRD GTYGEGEQGV
TIVELRD