MUTS2_CALBD
ID MUTS2_CALBD Reviewed; 787 AA.
AC B9MK78;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Athe_1642;
OS Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
OS (Anaerocellum thermophilum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX NCBI_TaxID=521460;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kataeva I., Adams M.W.W.;
RT "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL Submitted (JAN-2009) 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; CP001393; ACM60736.1; -; Genomic_DNA.
DR RefSeq; WP_015908069.1; NC_012034.1.
DR AlphaFoldDB; B9MK78; -.
DR SMR; B9MK78; -.
DR STRING; 521460.Athe_1642; -.
DR EnsemblBacteria; ACM60736; ACM60736; Athe_1642.
DR GeneID; 31772991; -.
DR KEGG; ate:Athe_1642; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000007723; 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_1000192209"
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; 89398 MW; 8D926370A973C928 CRC64;
MNQKTLKALE YDKIVEILKN MAKSTPAKEY FENLIPSTNV ADIENELNKV DESYRYVLKY
GNLPTLEFEN ILPSLKKSKL GATLNPHEIL QIGKVLKLSY EMRTYLSFTQ DFSFLESMKK
RLVNLKEVIS RIDQTFLTPD EILDTASSKL KEIRDKIRKL ENKIRDELNS MIRDPKIQRF
LQEPIITIRG EKLLLPVKAE FRNEVKGIVH DQSATGATLF VEPFVCVEIS NQIKILKNQE
KEEIERILQE ISSLIASYCE VIETSFYALV ELDIVFTKAI WAKEMNASKP IINASGIINL
KKARHPLIQK DKVVPIDIHL GKDFDVLIIT GPNTGGKTVT LKTVGLFCLL CQSGIFIPAD
EGSELCIFQK IFADIGDDQS IVQSLSTFSA HMKNIIEITK NADDKTLVLL DEIGAGTDPE
EGAALAKAIL KYLSEKGSKV IATTHYGELK IFAQQEDRFE NASCEFDVKT LKPTYRLLIG
IPGRSNALVI SSNLGLDKGI VEMARGYLSQ KTIDLDRIIN EMEQKRKEAE ENLELAQKLK
HEAQALKAAY EEEKKRFETE RERIRKKAIN EAKEIVESSQ YEIENLFKDL RKLAENLKEK
EVLKELEEKK REYERLIQSI SQQVKQEAES KTKKTIQNLR LGQKVYVRSF DAEGFVESLP
DSKGNLTVQI GIMKINVNLS DIEEVEGQDS KIYQIASRNV IIKEKNIDMS IDVRGKTSDD
AILEVDKYLD DAYTAGLKQV TIIHGKGTGV LRQAIRNFLR RHPHVKSFRD GTYGEGEQGV
TVVELKD