ID   NRDR_DEIDV              Reviewed;         148 AA.
AC   C1D0D5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Transcriptional repressor NrdR {ECO:0000255|HAMAP-Rule:MF_00440};
GN   Name=nrdR {ECO:0000255|HAMAP-Rule:MF_00440}; OrderedLocusNames=Deide_04740;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
CC   -!- FUNCTION: Negatively regulates transcription of bacterial
CC       ribonucleotide reductase nrd genes and operons by binding to NrdR-
CC       boxes. {ECO:0000255|HAMAP-Rule:MF_00440}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00440};
CC       Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00440};
CC   -!- SIMILARITY: Belongs to the NrdR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00440}.
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DR   EMBL; CP001114; ACO45309.1; -; Genomic_DNA.
DR   RefSeq; WP_012692432.1; NC_012526.1.
DR   AlphaFoldDB; C1D0D5; -.
DR   SMR; C1D0D5; -.
DR   STRING; 546414.Deide_04740; -.
DR   PaxDb; C1D0D5; -.
DR   EnsemblBacteria; ACO45309; ACO45309; Deide_04740.
DR   KEGG; ddr:Deide_04740; -.
DR   eggNOG; COG1327; Bacteria.
DR   HOGENOM; CLU_108412_0_0_0; -.
DR   OMA; YRFTTYE; -.
DR   OrthoDB; 1551627at2; -.
DR   Proteomes; UP000002208; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00440; NrdR; 1.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR003796; RNR_NrdR-like.
DR   PANTHER; PTHR30455; PTHR30455; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   TIGRFAMs; TIGR00244; TIGR00244; 1.
DR   PROSITE; PS51161; ATP_CONE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..148
FT                   /note="Transcriptional repressor NrdR"
FT                   /id="PRO_1000206112"
FT   DOMAIN          49..136
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00440"
FT   ZN_FING         3..34
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00440"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   148 AA;  16999 MW;  1367A96D4859CC0B CRC64;
     MKCPYCSAPD SKVVNSRPSD DGASIRRRRE CLNCARRFTT YERAQLEPLM VVKRSGPREA
     FNPDKLLRGL TLATEKRPVD ADALRAFAYG FEDDVQASEI HSEEIGKRAM TFLRPLDDVA
     YIRFASVYRD FDSLERFIEE IRGLKDQS