ARGR_THESQ
ID ARGR_THESQ Reviewed; 152 AA.
AC B1L9B6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Arginine repressor {ECO:0000255|HAMAP-Rule:MF_00173};
GN Name=argR {ECO:0000255|HAMAP-Rule:MF_00173}; OrderedLocusNames=TRQ2_0560;
OS Thermotoga sp. (strain RQ2).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC unclassified Thermotoga.
OX NCBI_TaxID=126740;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RQ2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga sp. RQ2.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000969; ACB08914.1; -; Genomic_DNA.
DR RefSeq; WP_004083185.1; NC_010483.1.
DR AlphaFoldDB; B1L9B6; -.
DR SMR; B1L9B6; -.
DR EnsemblBacteria; ACB08914; ACB08914; TRQ2_0560.
DR KEGG; trq:TRQ2_0560; -.
DR HOGENOM; CLU_097103_0_0_0; -.
DR OMA; IMGTICG; -.
DR OrthoDB; 1640037at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001687; 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 Repressor; Transcription; Transcription regulation.
FT CHAIN 1..152
FT /note="Arginine repressor"
FT /id="PRO_1000097894"
SQ SEQUENCE 152 AA; 17222 MW; BCD5384934D490E9 CRC64;
MKISKKRRQE LIRKIIHEKK ISNQFQIVEE LKKYGIKAVQ PTVARDLKEI GAVKIMDESG
NYVYKLLDET PVIDPWKELK RNFKSFVESI DRAGNLIVIK TIPGTASGIA RVIDRLDIDE
IVGTLAGDDT IFVAVRDPES CEKIVEKLSS IL