RECR_CALS8
ID RECR_CALS8 Reviewed; 199 AA.
AC A4XJV1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017};
GN Name=recR {ECO:0000255|HAMAP-Rule:MF_00017}; OrderedLocusNames=Csac_1594;
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: May play a role in DNA repair. It seems to be involved in an
CC RecBC-independent recombinational process of DNA repair. It may act
CC with RecF and RecO. {ECO:0000255|HAMAP-Rule:MF_00017}.
CC -!- SIMILARITY: Belongs to the RecR family. {ECO:0000255|HAMAP-
CC Rule:MF_00017}.
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DR EMBL; CP000679; ABP67186.1; -; Genomic_DNA.
DR RefSeq; WP_011917122.1; NC_009437.1.
DR AlphaFoldDB; A4XJV1; -.
DR SMR; A4XJV1; -.
DR STRING; 351627.Csac_1594; -.
DR EnsemblBacteria; ABP67186; ABP67186; Csac_1594.
DR KEGG; csc:Csac_1594; -.
DR eggNOG; COG0353; Bacteria.
DR HOGENOM; CLU_060739_1_0_9; -.
DR OMA; DVMAIEN; -.
DR OrthoDB; 1661836at2; -.
DR Proteomes; UP000000256; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd01025; TOPRIM_recR; 1.
DR HAMAP; MF_00017; RecR; 1.
DR InterPro; IPR000093; DNA_Rcmb_RecR.
DR InterPro; IPR023627; Rcmb_RecR.
DR InterPro; IPR023628; Rcmb_RecR_C4-type_Zn.
DR InterPro; IPR015967; Rcmb_RecR_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034137; TOPRIM_RecR.
DR PANTHER; PTHR30446; PTHR30446; 1.
DR Pfam; PF02132; RecR; 1.
DR Pfam; PF13662; Toprim_4; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF111304; SSF111304; 1.
DR TIGRFAMs; TIGR00615; recR; 1.
DR PROSITE; PS01300; RECR; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Metal-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..199
FT /note="Recombination protein RecR"
FT /id="PRO_0000322874"
FT DOMAIN 81..176
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
FT ZN_FING 58..73
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
SQ SEQUENCE 199 AA; 21990 MW; BA29B1C510306A8B CRC64;
MQAKENAISK LIQQLEKLPG IGQKTAQRLA FYIINMKNED VKALAEAILS AKNSTKLCKI
CCNFTEGDIC HICSDDKRDR SIICVVEEPQ DVVALEKVKE YKGLYHVLHG AISPLKGKYP
EQLTIDVLLK RLADTNVKEV IIATNPDVDG EATASYLARL IKPMGIKVTR IARGIPVGGD
IEYADEVTIL KAIEGRKEI