ID A0A2N2A4N4_9FIRM Unreviewed; 149 AA. AC A0A2N2A4N4; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 07-NOV-2018, entry version 5. DE RecName: Full=Arginine repressor {ECO:0000256|HAMAP-Rule:MF_00173}; GN Name=argR {ECO:0000256|HAMAP-Rule:MF_00173}; GN ORFNames=CVV04_05670 {ECO:0000313|EMBL:PKM40679.1}; OS Firmicutes bacterium HGW-Firmicutes-9. OC Bacteria; Firmicutes. OX NCBI_TaxID=2013790 {ECO:0000313|EMBL:PKM40679.1}; RN [1] {ECO:0000313|EMBL:PKM40679.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGW-Firmicutes-9 {ECO:0000313|EMBL:PKM40679.1}; RX PubMed=28350393; DOI=.1038/ismej.2017.39; RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., RA Anantharaman K., Probst A., Burstein D., Thomas B.C., Banfield J.F.; RT "Potential for microbial H2 and metal transformations associated with RT novel bacteria and archaea in deep terrestrial subsurface sediments."; RL ISME J. 11:1915-1929(2017). RN [2] {ECO:0000313|EMBL:PKM40679.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGW-Firmicutes-9 {ECO:0000313|EMBL:PKM40679.1}; RA Han C.G.; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Regulates arginine biosynthesis genes. CC {ECO:0000256|HAMAP-Rule:MF_00173}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis CC [regulation]. {ECO:0000256|HAMAP-Rule:MF_00173}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00173, CC ECO:0000256|SAAS:SAAS00347855}. CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000256|HAMAP- CC Rule:MF_00173, ECO:0000256|SAAS:SAAS00542412}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PKM40679.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PGZM01000002; PKM40679.1; -; Genomic_DNA. DR UniPathway; UPA00068; -. 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 ProDom; PD007402; Arg_repress; 1. 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 {ECO:0000256|HAMAP-Rule:MF_00173}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00173}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00173, KW ECO:0000256|SAAS:SAAS00347849}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00173, KW ECO:0000256|SAAS:SAAS00347870}; KW Repressor {ECO:0000256|HAMAP-Rule:MF_00173}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00173, KW ECO:0000256|SAAS:SAAS00347853}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00173, KW ECO:0000256|SAAS:SAAS00347854}. FT DOMAIN 2 66 Arg_repressor. {ECO:0000259|Pfam: FT PF01316}. FT DOMAIN 79 145 Arg_repressor_C. {ECO:0000259|Pfam: FT PF02863}. SQ SEQUENCE 149 AA; 16465 MW; E87CCC2740D5435B CRC64; MKAKRHDMIS KLIASENIET QEELAGKLRD HGFSVTQATV SRDIKELRLI KVLTPEGRYR YATVEKAEAD LQERFIRMFS NCVLSVTSAG NLIVIKTIAG SANAAAEAVD TLKWPDILGS IAGDNTIFIA VRDAKSVGDI IKKFQKMLK //