RECR_LEPIN
ID RECR_LEPIN Reviewed; 201 AA.
AC Q8EY84;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017};
GN Name=recR {ECO:0000255|HAMAP-Rule:MF_00017}; OrderedLocusNames=LA_4333;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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; AE010300; AAN51531.1; -; Genomic_DNA.
DR RefSeq; NP_714513.1; NC_004342.2.
DR RefSeq; WP_000829688.1; NC_004342.2.
DR AlphaFoldDB; Q8EY84; -.
DR SMR; Q8EY84; -.
DR STRING; 189518.LA_4333; -.
DR EnsemblBacteria; AAN51531; AAN51531; LA_4333.
DR GeneID; 61143336; -.
DR KEGG; lil:LA_4333; -.
DR PATRIC; fig|189518.3.peg.4303; -.
DR HOGENOM; CLU_060739_1_0_12; -.
DR InParanoid; Q8EY84; -.
DR OMA; DVMAIEN; -.
DR Proteomes; UP000001408; Chromosome I.
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..201
FT /note="Recombination protein RecR"
FT /id="PRO_0000190341"
FT DOMAIN 83..178
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
FT ZN_FING 60..75
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
SQ SEQUENCE 201 AA; 22706 MW; 4F7B4DD80AA9BB65 CRC64;
MAENLANHLL DEMIEALSSL PGIGRKSAFR ISFHLLRLEQ GLFNQFIHQL TDTKNKIKFC
KRCGSYAETE ICEICVSEKR DSHTFCVVEQ PEDIFFIENT REFQGKYHVL NGVISPLEGI
GPRDLRIKEL LERIEPEQVK EVLIATNPTL EGDATADYLA NQLKPISVNV TRIAYGITVG
GSIELADQYT LGRAIRSRLQ L