ID   ARGR_DEIDV              Reviewed;         157 AA.
AC   C1CYD7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Arginine repressor {ECO:0000255|HAMAP-Rule:MF_00173};
GN   Name=argR {ECO:0000255|HAMAP-Rule:MF_00173}; OrderedLocusNames=Deide_01490;
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: Regulates arginine biosynthesis genes. {ECO:0000255|HAMAP-
CC       Rule:MF_00173}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00173}.
CC   -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00173}.
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DR   EMBL; CP001114; ACO44958.1; -; Genomic_DNA.
DR   RefSeq; WP_012692081.1; NC_012526.1.
DR   AlphaFoldDB; C1CYD7; -.
DR   SMR; C1CYD7; -.
DR   STRING; 546414.Deide_01490; -.
DR   PaxDb; C1CYD7; -.
DR   PRIDE; C1CYD7; -.
DR   EnsemblBacteria; ACO44958; ACO44958; Deide_01490.
DR   KEGG; ddr:Deide_01490; -.
DR   eggNOG; COG1438; Bacteria.
DR   HOGENOM; CLU_097103_3_0_0; -.
DR   OMA; IMGTICG; -.
DR   OrthoDB; 1640037at2; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000002208; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0034618; F:arginine binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_00173; Arg_repressor; 1.
DR   InterPro; IPR001669; Arg_repress.
DR   InterPro; IPR020899; Arg_repress_C.
DR   InterPro; IPR036251; Arg_repress_C_sf.
DR   InterPro; IPR020900; Arg_repress_DNA-bd.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR34471; PTHR34471; 1.
DR   Pfam; PF01316; Arg_repressor; 1.
DR   Pfam; PF02863; Arg_repressor_C; 1.
DR   PRINTS; PR01467; ARGREPRESSOR.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF55252; SSF55252; 1.
DR   TIGRFAMs; TIGR01529; argR_whole; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; DNA-binding;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..157
FT                   /note="Arginine repressor"
FT                   /id="PRO_1000203712"
SQ   SEQUENCE   157 AA;  17759 MW;  42E643CA00FD1F93 CRC64;
     MVSKELSKEQ RQKRIQDIIA RESISTQGEL VQRLRADNIQ VTQATISRDI NELRLVRLPI
     GKGRHRYALA QMTGHTDVEE ELGRLFQNFV HDVDRGENML VIRTADGHAT GVALLLDRLR
     RDDIVGTLAG EDTIFVVART TLEAESLMEE FHALMLG