ID SYR_GEOMG Reviewed; 562 AA. AC Q39VQ6; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 27-MAR-2024, entry version 105. 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=Gmet_1434; OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15). OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=269799; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 53774 / DSM 7210 / GS-15; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Geobacter metallireducens GS-15."; RL Submitted (OCT-2005) 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 -!- SEQUENCE CAUTION: CC Sequence=ABB31668.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CP000148; ABB31668.1; ALT_INIT; Genomic_DNA. DR AlphaFoldDB; Q39VQ6; -. DR SMR; Q39VQ6; -. DR STRING; 269799.Gmet_1434; -. DR KEGG; gme:Gmet_1434; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_0_1_7; -. DR Proteomes; UP000007073; 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; cd07956; Anticodon_Ia_Arg; 1. 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..562 FT /note="Arginine--tRNA ligase" FT /id="PRO_0000242026" FT MOTIF 130..140 FT /note="'HIGH' region" SQ SEQUENCE 562 AA; 62252 MW; 04F8CEB87823CC87 CRC64; MKDRVRSLVA EGIERCFADG SLASNQMPAI VIEKPAHAEH GDFACTVAMS MAKAERKAPR VIAETIVKHI ENGESGIIGG IDIAGPGFIN FRIKNEAWSR TLAVVEAAGA SFGRSCAGEE RKVQVEFVSA NPTGPLHIGH GRGAAIGDTI CRLLSASGFD VTREFYYNDA GAQIANLALS VQSRCLGIEP GDPRWPADGY QGDYIKDVAR SYLNRETVDA GDQHVTAAGD PNDLDAIRRF AVAYLRREQD QDLLAFDVHF DVYSLESSLY TEGRVEEVVR RLIENGHTFE QDGALWLRTT DFGDDKDRVM RKSDGSYTYF VPDVAYHLAK WERGFTRVIN EQGADHHSTI TRVRAGLQAL NAGIPQEWPE YVLHQMVTVM RGGEEVKISK RAGSYVTLRD LIDEVGRDAT RFFFLMRKPD SQLVFDIDLA KQQSLENPVY YVQYAHARIS SIFEAACDRG ISVPSFPDAH VDLLETPEEI ELIKLIGSFP EVIEGSALSF EPHRITYYLQ ELAGAFHSFY NKNRVIGEGK ELSSARLFLL KGVAQVLKNG LALLGVSAPE KM //