ID SYR_RHILW Reviewed; 585 AA. AC B5ZMF2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 94. 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=Rleg2_1482; OS Rhizobium leguminosarum bv. trifolii (strain WSM2304). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=395492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM2304; RX PubMed=21304679; DOI=10.4056/sigs.44642; RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R., RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M., RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M., RA Yates R., Howieson J.; RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain RT WSM2304, an effective microsymbiont of the South American clover Trifolium RT polymorphum."; RL Stand. Genomic Sci. 2:66-76(2010). 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; CP001191; ACI54774.1; -; Genomic_DNA. DR RefSeq; WP_012557480.1; NC_011369.1. DR AlphaFoldDB; B5ZMF2; -. DR SMR; B5ZMF2; -. DR STRING; 395492.Rleg2_1482; -. DR KEGG; rlt:Rleg2_1482; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_0_1_5; -. DR Proteomes; UP000008330; 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; 2. 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. FT CHAIN 1..585 FT /note="Arginine--tRNA ligase" FT /id="PRO_1000095397" FT MOTIF 131..141 FT /note="'HIGH' region" SQ SEQUENCE 585 AA; 64760 MW; 24C8EA29D6D884D3 CRC64; MNLFTDFEAR IKTALEQIDL VREKRSELDF GRIAVEPPRD ASHGDVATNA AMVLAKPLGT NPRALADIII AKLREDADVA DVSVAGPGFI NIRLAVGYWQ RLLAAMIGAG TDYGRSTLGE GRKVNVEYVS ANPTGPMHVG HCRGAVVGDA LANLLAFAGY GVEKEYYIND AGSQIDVLAR SVFLRYREAL GEKIGEIPSG LYPGDYLVPV GQSLAADYGV RLHNMPEDQW MPIVKDRTID AMMVMIREDL ASLNVHHDIF FSERTLHANG AAAIRTAIND LTFKGYVYKG TLPPPKGQLP EDWEDREQTL FRSTEVGDDM DRPLIKSDGS YTYFAADVAY FKNKFDRGFD EMIYVLGADH GGYVKRLEAV ARGVSDGKAK LTVLLCQLVK LYRNGEPVKM SKRSGDFVTL RDVVEEVGSD SVRFMMLYRK NSEPLDFDFA KVTEQSKDNP VFYVQYAHAR CMSVFRQARE AFGDLDVSPE EFAQTVAGIG DPAELQLVAK LAEFPRIVEA AAQSQEPHRL AFYLYDLASS FHAHWNKGKD QPELRFVNDK NRESTIARLG LVYAVASVLK SGLAITGTAA PDEMR //