ID A0LUC0_ACIC1 Unreviewed; 184 AA.
AC A0LUC0;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Arginine repressor {ECO:0000256|ARBA:ARBA00021148, ECO:0000256|HAMAP-Rule:MF_00173};
GN Name=argR {ECO:0000256|HAMAP-Rule:MF_00173};
GN OrderedLocusNames=Acel_1258 {ECO:0000313|EMBL:ABK53030.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK53030.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|EMBL:ABK53030.1, ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B
RC {ECO:0000313|Proteomes:UP000008221};
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
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}.
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DR EMBL; CP000481; ABK53030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0LUC0; -.
DR SMR; A0LUC0; -.
DR STRING; 351607.Acel_1258; -.
DR KEGG; ace:Acel_1258; -.
DR eggNOG; COG1438; Bacteria.
DR HOGENOM; CLU_097103_1_1_11; -.
DR InParanoid; A0LUC0; -.
DR OrthoDB; 7060358at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000008221; 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; 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 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:UP000008221};
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 8..73
FT /note="Arginine repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01316"
FT DOMAIN 89..153
FT /note="Arginine repressor C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02863"
FT REGION 164..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 184 AA; 19200 MW; 2DF880973442A83D CRC64;
MTTATPGTKA ARHARIRELL AARSIRSQHE LAELLAAEGF LVTQATLSRD LEEIGAVRLR
SVDGGFVYVV PSTEPPAASA AGRLARLAAE LLISAEPSGN LVVVRTPPGG AHLLASAMDQ
AGLPDLLGTV AGDDTVLCVV RRPDGGAALA RRLLDLAQRR GALTRARKRS ASPHAGAEHE
GEIR
//
