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Database: UniProt
Entry: A0A420VEF3_9BACI
LinkDB: A0A420VEF3_9BACI
Original site: A0A420VEF3_9BACI 
ID   A0A420VEF3_9BACI        Unreviewed;       150 AA.
AC   A0A420VEF3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   18-JUN-2025, entry version 15.
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=Cdeb_00766 {ECO:0000313|EMBL:RKO62034.1};
OS   Caldibacillus debilis GB1.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Caldibacillus.
OX   NCBI_TaxID=1339248 {ECO:0000313|EMBL:RKO62034.1, ECO:0000313|Proteomes:UP000286235};
RN   [1] {ECO:0000313|EMBL:RKO62034.1, ECO:0000313|Proteomes:UP000286235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB1 {ECO:0000313|EMBL:RKO62034.1,
RC   ECO:0000313|Proteomes:UP000286235};
RA   Wushke S.T., Zhang X., Fristensky B., Wilkins J.A., Levin D.B.,
RA   Sparling R.;
RT   "Genome and proteome characterization of Caldibacillus debilis GB1 derived
RT   from a cellulolytic aero-tolerant co-culture.";
RL   Submitted (DEC-2013) 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:RKO62034.1}.
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DR   EMBL; AZRV01000023; RKO62034.1; -; Genomic_DNA.
DR   RefSeq; WP_120668289.1; NZ_AZRV01000023.1.
DR   AlphaFoldDB; A0A420VEF3; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000286235; 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; NF003281; PRK04280.1; 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:UP000286235};
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..69
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;  17076 MW;  52642E9A08299394 CRC64;
     MNKEKRHFKI KELIQKYEIK TQDELVHYLS KEGFHVTQAT VSRDLKELHL VKVPSPDGGY
     KYSLTQEQNV SVVPKLQKLL TDVLVKVDFA QHLVVLKTIP GNAHPVGVLI DQLDWKEIVG
     TVCGDDTCLI ITRNNGDASK LTKRFRELLT
//
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