ID A0A4V6NZ66_9FIRM Unreviewed; 150 AA.
AC A0A4V6NZ66;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=Arginine repressor {ECO:0000256|HAMAP-Rule:MF_00173, ECO:0000256|NCBIfam:TIGR01529};
GN Name=argR {ECO:0000256|HAMAP-Rule:MF_00173};
GN ORFNames=EDD65_102289 {ECO:0000313|EMBL:TCS91354.1};
OS Keratinibaculum paraultunense.
OC Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
OC Tepidimicrobiaceae; Keratinibaculum.
OX NCBI_TaxID=1278232 {ECO:0000313|EMBL:TCS91354.1, ECO:0000313|Proteomes:UP000294567};
RN [1] {ECO:0000313|EMBL:TCS91354.1, ECO:0000313|Proteomes:UP000294567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26752 {ECO:0000313|EMBL:TCS91354.1,
RC ECO:0000313|Proteomes:UP000294567};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates arginine biosynthesis genes. {ECO:0000256|HAMAP-
CC Rule:MF_00173}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC {ECO:0000256|HAMAP-Rule:MF_00173}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00173}.
CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000256|ARBA:ARBA00008316,
CC ECO:0000256|HAMAP-Rule:MF_00173}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TCS91354.1}.
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DR EMBL; SMAE01000002; TCS91354.1; -; Genomic_DNA.
DR RefSeq; WP_132026146.1; NZ_CP068564.1.
DR AlphaFoldDB; A0A4V6NZ66; -.
DR OrthoDB; 9807089at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000294567; Unassembled WGS sequence.
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:L-arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR GO; GO:1900079; P:regulation of arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 NCBIfam; TIGR01529; argR_whole; 1.
DR NCBIfam; NF001680; PRK00441.1; 1.
DR PANTHER; PTHR34471; ARGININE REPRESSOR; 1.
DR PANTHER; PTHR34471:SF1; ARGININE REPRESSOR; 1.
DR Pfam; PF01316; Arg_repressor; 1.
DR Pfam; PF02863; Arg_repressor_C; 1.
DR PRINTS; PR01467; ARGREPRESSOR.
DR SUPFAM; SSF55252; C-terminal domain of arginine repressor; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00173};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00173};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00173};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00173}; Reference proteome {ECO:0000313|Proteomes:UP000294567};
KW Repressor {ECO:0000256|HAMAP-Rule:MF_00173};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00173};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_00173}.
FT DOMAIN 1..65
FT /note="Arginine repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01316"
FT DOMAIN 80..146
FT /note="Arginine repressor C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02863"
SQ SEQUENCE 150 AA; 16799 MW; EE4F73D9B9282A98 CRC64;
MNKYTRQRII LNLINKYEIE TQEELAEHLL KQGIDITQAT ISRDIKELRL VKVLTNTGKY
KYATIDTSHK GIYQRLNNIF KSSVLNVEVA ENIVVVKTLP GAAQVCASAI DNFNIEGVVG
TIAGDDTIFV AIQNIDLMDH VLTSIQNLLK
//
