ID A0A1P8YCU8_9NOCA Unreviewed; 202 AA.
AC A0A1P8YCU8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Recombination protein RecR {ECO:0000256|HAMAP-Rule:MF_00017};
GN Name=recR {ECO:0000256|HAMAP-Rule:MF_00017,
GN ECO:0000313|EMBL:AQA21818.1};
GN ORFNames=BTZ20_5545 {ECO:0000313|EMBL:AQA21818.1};
OS Rhodococcus sp. MTM3W5.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1805827 {ECO:0000313|EMBL:AQA21818.1, ECO:0000313|Proteomes:UP000187995};
RN [1] {ECO:0000313|EMBL:AQA21818.1, ECO:0000313|Proteomes:UP000187995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTM3W5.2 {ECO:0000313|EMBL:AQA21818.1,
RC ECO:0000313|Proteomes:UP000187995};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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:0000256|HAMAP-Rule:MF_00017}.
CC -!- SIMILARITY: Belongs to the RecR family. {ECO:0000256|HAMAP-
CC Rule:MF_00017}.
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DR EMBL; CP019572; AQA21818.1; -; Genomic_DNA.
DR RefSeq; WP_027501651.1; NZ_CP019572.1.
DR AlphaFoldDB; A0A1P8YCU8; -.
DR STRING; 1805827.BTZ20_5545; -.
DR OrthoDB; 9802672at2; -.
DR Proteomes; UP000187995; 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; cd00080; H3TH_StructSpec-5'-nucleases; 1.
DR CDD; cd01025; TOPRIM_recR; 1.
DR Gene3D; 3.30.60.80; -; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 6.10.250.240; -; 1.
DR Gene3D; 1.10.8.420; RecR Domain 1; 1.
DR HAMAP; MF_00017; RecR; 1.
DR InterPro; IPR000093; DNA_Rcmb_RecR.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR023627; Rcmb_RecR.
DR InterPro; IPR015967; Rcmb_RecR_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034137; TOPRIM_RecR.
DR NCBIfam; TIGR00615; recR; 1.
DR PANTHER; PTHR30446; RECOMBINATION PROTEIN RECR; 1.
DR PANTHER; PTHR30446:SF0; RECOMBINATION PROTEIN RECR; 1.
DR Pfam; PF21175; RecR_C; 1.
DR Pfam; PF21176; RecR_HhH; 1.
DR Pfam; PF02132; RecR_ZnF; 1.
DR Pfam; PF13662; Toprim_4; 1.
DR SMART; SM00278; HhH1; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF111304; Recombination protein RecR; 1.
DR PROSITE; PS01300; RECR; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00017};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW Rule:MF_00017};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00017};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00017};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00017};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_00017}.
FT DOMAIN 79..179
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 56..71
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00017"
SQ SEQUENCE 202 AA; 22138 MW; 2E0F6B8876EB3D93 CRC64;
MYEGPVQDLI DELGKLPGIG PKSAQRIAFH LLSVEPPDID RLQNALQRVR DGVQFCVVCG
TVSDKEKCRI CADARRDRTV ICVVEEPKDV QAVERTREFR GRYHVLGGAL DPLSGVGPDQ
LRIRELLARI GNQEDGVDVS EVIIATDPNT EGEATATYLV RMLRDFPGLT VSRLASGLPM
GGDLEFADEL TLGRALSGRR TL
//
