ID SYR_SHEB5 Reviewed; 581 AA. AC A3D9A3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 85. 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=Sbal_3845; OS Shewanella baltica (strain OS155 / ATCC BAA-1091). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=325240; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS155 / ATCC BAA-1091; 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 Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I., RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.; RT "Complete sequence of chromosome of Shewanella baltica OS155."; RL Submitted (FEB-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; CP000563; ABN63316.1; -; Genomic_DNA. DR RefSeq; WP_011847952.1; NC_009052.1. DR AlphaFoldDB; A3D9A3; -. DR SMR; A3D9A3; -. DR STRING; 325240.Sbal_3845; -. DR KEGG; sbl:Sbal_3845; -. DR HOGENOM; CLU_006406_5_1_6; -. DR OrthoDB; 9803211at2; -. DR Proteomes; UP000001557; 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. FT CHAIN 1..581 FT /note="Arginine--tRNA ligase" FT /id="PRO_1000018112" FT MOTIF 126..136 FT /note="'HIGH' region" SQ SEQUENCE 581 AA; 64864 MW; 65D884BA41BC92D1 CRC64; MKSHIQSLLE QTLESFKQQG IVPADFEARI QVDRTKDKSH GDLATNLAMM LTKVAGKNPR ELAQLIIDTL PASAYVAKVE IAGPGFINFF INDSALADQL QNAVNDEHLG IKLPTPQTVV VDYSSPNLAK EMHVGHLRST IIGDSVVRAL EFLGHKVIRQ NHVGDWGTQF GMLLAYMEEL RAKNGEKAQL ELSDLENFYR AAKLRFDESA EFATRARQLV VELQSGDEYC NKLWREFNDI SLSHCHEVYA RLGVSLTRAD VHGESAYNAD LEQVVKDLDA QGLLTESNGA KVVFQEAFRN KEGEPLPVII QKADGGYLYA TSDLAAMRYR SNVLKADRVL YFVDLRQALH FQQVFSLAKL AKFVREDMSL EHLGFGTMNG EDGRPFKTRS GGVVKLVDLL EEANVRALEL VRSKNPDMDE ATLTEIARVV GISAVKYADL SKNRTSDYIF SFEQMLSFEG NTAPYLLYAY TRVAGIFKRV TDLDLSQAKI VLEHEKEKDL GNKLAQFGEI LSRVVDKGQP HVLCAYLYEL AGAFSSFYEA CPVLAADNDA QKNSRLLLAQ LTARTLQKGL NLLGIETLER M //