ID SYR_GEOUR Reviewed; 561 AA. AC A5G3W5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 90. DE RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123}; DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123}; DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123}; DE Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123}; GN Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; GN OrderedLocusNames=Gura_2304; OS Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens). OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales; OC Geobacteraceae; Geotalea. OX NCBI_TaxID=351605; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1134 / JCM 13001 / Rf4; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M., RA Lovley D., Richardson P.; RT "Complete sequence of Geobacter uraniireducens Rf4."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl- CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA- CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215; CC EC=6.1.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00123}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00123}. 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; CP000698; ABQ26483.1; -; Genomic_DNA. DR RefSeq; WP_011939177.1; NC_009483.1. DR AlphaFoldDB; A5G3W5; -. DR SMR; A5G3W5; -. DR STRING; 351605.Gura_2304; -. DR KEGG; gur:Gura_2304; -. DR HOGENOM; CLU_006406_0_1_7; -. DR OrthoDB; 9803211at2; -. DR Proteomes; UP000006695; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00671; ArgRS_core; 1. DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00123; Arg_tRNA_synth; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR001278; Arg-tRNA-ligase. DR InterPro; IPR005148; Arg-tRNA-synth_N. DR InterPro; IPR036695; Arg-tRNA-synth_N_sf. DR InterPro; IPR035684; ArgRS_core. DR InterPro; IPR008909; DALR_anticod-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR NCBIfam; TIGR00456; argS; 1. DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1. DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1. DR Pfam; PF03485; Arg_tRNA_synt_N; 1. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF00750; tRNA-synt_1d; 1. DR PRINTS; PR01038; TRNASYNTHARG. DR SMART; SM01016; Arg_tRNA_synt_N; 1. DR SMART; SM00836; DALR_1; 1. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..561 FT /note="Arginine--tRNA ligase" FT /id="PRO_1000076216" FT MOTIF 129..139 FT /note="'HIGH' region" SQ SEQUENCE 561 AA; 62651 MW; E0262C1DD274788B CRC64; MKELLRDLIT KELASCFADG SLSSGVFPSI VIEKPAHAEH GDFATNVAML LAKAEKKAPR VVAEILVSRL QESADICSKL EVAGPGFINF YVKDEAWRQT LIAIDRACAD YGKSRIGEGK KIQVEFVSAN PTGPLHIGHG RGAAIGDTIC RLLAAIGWDV TREFYYNDAG QQIANLALSV QARCLGIEPD DPRWPLDGYQ GDYIRDVARS YLGQETVEAD DQHVTAAGDP QDLDAIRRFA VAYLRREQDQ DLTAFDVHFD VYSLESALYA EGRVEAVVQR LIDSGHTYEQ DGALWLRTTT FGDDKDRVMR KADGGYTYFV PDVAYHLSKW ERGFTRVINE QGADHHSTIT RVRAGLQALN AGIPVGWPEY VLHQMVTVMR GGEEVKISKR AGSYVTLRDL IDEVGRDATR FFFVMRKPDS QLVFDIDLAK QQTLDNPVYY VQYAHARICS IFENALERGF VLPAAESVPL ERLVTLEEMT IIKTLASFPE ILEGSALNFE PHRVTYYLQE LAGQFHSFYN RNRVITEDAE LTAARLFLLK CVALTLKNAL TVLGISAPEK M //