RECR_DEIRA
ID RECR_DEIRA Reviewed; 220 AA.
AC Q9ZNA2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017};
GN Name=recR {ECO:0000255|HAMAP-Rule:MF_00017}; OrderedLocusNames=DR_0198;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=11056289; DOI=10.1016/s0921-8777(00)00044-6;
RA Kitayama S., Narumi I., Kikuchi M., Watanabe H.;
RT "Mutation in recR gene of Deinococcus radiodurans and possible involvement
RT of its product in the repair of DNA interstrand cross-links.";
RL Mutat. Res. 461:179-187(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AB020240; BAA34648.1; -; Genomic_DNA.
DR EMBL; AE000513; AAF09785.1; -; Genomic_DNA.
DR PIR; H75547; H75547.
DR RefSeq; NP_293922.1; NC_001263.1.
DR RefSeq; WP_010886844.1; NZ_CP015081.1.
DR PDB; 1VDD; X-ray; 2.50 A; A/B/C/D=1-220.
DR PDB; 2V1C; X-ray; 3.80 A; A/B=1-220.
DR PDB; 4JCV; X-ray; 3.34 A; A/B/C/D=2-220.
DR PDBsum; 1VDD; -.
DR PDBsum; 2V1C; -.
DR PDBsum; 4JCV; -.
DR AlphaFoldDB; Q9ZNA2; -.
DR SMR; Q9ZNA2; -.
DR IntAct; Q9ZNA2; 1.
DR MINT; Q9ZNA2; -.
DR STRING; 243230.DR_0198; -.
DR DrugBank; DB03366; Imidazole.
DR EnsemblBacteria; AAF09785; AAF09785; DR_0198.
DR KEGG; dra:DR_0198; -.
DR PATRIC; fig|243230.17.peg.362; -.
DR eggNOG; COG0353; Bacteria.
DR HOGENOM; CLU_060739_1_0_0; -.
DR InParanoid; Q9ZNA2; -.
DR OMA; DVMAIEN; -.
DR OrthoDB; 1661836at2; -.
DR EvolutionaryTrace; Q9ZNA2; -.
DR Proteomes; UP000002524; 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:0006302; P:double-strand break repair; IMP:CACAO.
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 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..220
FT /note="Recombination protein RecR"
FT /id="PRO_0000190315"
FT DOMAIN 80..173
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
FT ZN_FING 57..72
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
FT REGION 190..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 88
FT /note="P -> H (in Ref. 1; BAA34648)"
FT /evidence="ECO:0000305"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:1VDD"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:1VDD"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1VDD"
FT HELIX 37..53
FT /evidence="ECO:0007829|PDB:1VDD"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1VDD"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1VDD"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:1VDD"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1VDD"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1VDD"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:1VDD"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:1VDD"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1VDD"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1VDD"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1VDD"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:1VDD"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1VDD"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:1VDD"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:1VDD"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4JCV"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1VDD"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:1VDD"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:1VDD"
SQ SEQUENCE 220 AA; 23723 MW; CAF60A203044EA0C CRC64;
MKYPPSLVSL IRELSRLPGI GPKSAQRLAF HLFEQPREDI ERLASALLEA KRDLHVCPIC
FNITDAEKCD VCADPSRDQR TICVVEEPGD VIALERSGEY RGLYHVLHGV LSPMNGVGPD
KLHIKPLLPR VGQGMEVILA TGTTVEGDAT ALYLQRLLEP LGAAISRIAY GVPVGGSLEY
TDEVTLGRAL TGRQTVSKPQ PPQRPGDEDG ADGAAVPASR
