ID   RECR_RHOJR              Reviewed;         202 AA.
AC   Q0S8Y4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017};
GN   Name=recR {ECO:0000255|HAMAP-Rule:MF_00017};
GN   OrderedLocusNames=RHA1_ro04211;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG96002.1; -; Genomic_DNA.
DR   RefSeq; WP_005248644.1; NC_008268.1.
DR   AlphaFoldDB; Q0S8Y4; -.
DR   SMR; Q0S8Y4; -.
DR   STRING; 101510.RHA1_ro04211; -.
DR   EnsemblBacteria; ABG96002; ABG96002; RHA1_ro04211.
DR   GeneID; 66783697; -.
DR   KEGG; rha:RHA1_ro04211; -.
DR   eggNOG; COG0353; Bacteria.
DR   HOGENOM; CLU_060739_1_0_11; -.
DR   OMA; DVMAIEN; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0140640; F:catalytic activity, acting on a nucleic acid; IEA:UniProt.
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;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..202
FT                   /note="Recombination protein RecR"
FT                   /id="PRO_0000322940"
FT   DOMAIN          79..179
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
FT   ZN_FING         56..71
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
SQ   SEQUENCE   202 AA;  22145 MW;  8B428C4C8DFE0034 CRC64;
     MYEGPVQDLI DELGKLPGVG PKSAQRIAFH LLSVEPPEID RLKNALQRVR DGVQFCVVCG
     TVSDKEHCRI CADPRRDRTV ICVVEEPKDV QAVERTREFK GRYHVLGGAL DPLSGVGPDQ
     LRIRELLARI GNQEDGVDVS EVIIATDPNT EGEATATYLV RMLRDFPGLT VSRLASGLPM
     GGDLEFADEL TLGRALSGRR TL