RECR_LEPBJ
ID RECR_LEPBJ Reviewed; 197 AA.
AC Q04NX9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, 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=LBJ_3003;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB197;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(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; CP000350; ABJ77391.1; -; Genomic_DNA.
DR RefSeq; WP_002732275.1; NC_008510.1.
DR AlphaFoldDB; Q04NX9; -.
DR SMR; Q04NX9; -.
DR EnsemblBacteria; ABJ77391; ABJ77391; LBJ_3003.
DR GeneID; 61175440; -.
DR KEGG; lbj:LBJ_3003; -.
DR HOGENOM; CLU_060739_1_0_12; -.
DR OMA; DVMAIEN; -.
DR Proteomes; UP000000656; Chromosome 1.
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..197
FT /note="Recombination protein RecR"
FT /id="PRO_0000322902"
FT DOMAIN 79..174
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 197 AA; 22253 MW; 353C6EB1CFACE04E CRC64;
MANHLLEEMV DALSSLPGIG RKSAFRISFH LLRLEQGHFN HFIHQLTNTK NKIKFCKRCG
SYAETEICNI CTSEKRDTHT FCVVEQPEDI FFIENTREFH GKYHVLNGVI SPLEGIGPKD
LRIKELLERI EPEQIKEVLV ATNPTLEGDA TADYLASQLK PLSVDVTRIA YGITVGGSIE
LADQYTLGRA IRSRLQL