RECR_MYCVP
ID RECR_MYCVP Reviewed; 203 AA.
AC A1TGJ3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-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=Mvan_5527;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
RG US DOE Joint Genome Institute;
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 Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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; CP000511; ABM16293.1; -; Genomic_DNA.
DR RefSeq; WP_011782646.1; NC_008726.1.
DR AlphaFoldDB; A1TGJ3; -.
DR SMR; A1TGJ3; -.
DR STRING; 350058.Mvan_5527; -.
DR EnsemblBacteria; ABM16293; ABM16293; Mvan_5527.
DR KEGG; mva:Mvan_5527; -.
DR eggNOG; COG0353; Bacteria.
DR HOGENOM; CLU_060739_1_0_11; -.
DR OMA; DVMAIEN; -.
DR OrthoDB; 1661836at2; -.
DR Proteomes; UP000009159; 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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; SM00278; HhH1; 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..203
FT /note="Recombination protein RecR"
FT /id="PRO_0000322918"
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 203 AA; 22017 MW; CCB84E44D241EB07 CRC64;
MFEGPVQDLI DELGKLPGIG PKSAQRIAFH LLSVEPPDID RLTAVLNKVR DGVTFCAVCG
NVSDEERCRI CGDARRDASL ICVVEEPKDV QAVERTREFR GRYHVLGGAL DPLSGIGPDQ
LRIRELLNRI GERVDGVEVA EVIIATDPNT EGEATATYLV RMLRDIPGLT VTRIASGLPM
GGDLEFADEL TLGRALAGRR AMA