ID SYR_FLAPJ Reviewed; 601 AA. AC A6GZP8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 88. 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}; OrderedLocusNames=FP1498; OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 / OS JIP02/86). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=402612; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86; RX PubMed=17592475; DOI=10.1038/nbt1313; RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B., RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F., RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.; RT "Complete genome sequence of the fish pathogen Flavobacterium RT psychrophilum."; RL Nat. Biotechnol. 25:763-769(2007). 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; AM398681; CAL43571.1; -; Genomic_DNA. DR RefSeq; WP_011963616.1; NC_009613.3. DR RefSeq; YP_001296380.1; NC_009613.3. DR AlphaFoldDB; A6GZP8; -. DR SMR; A6GZP8; -. DR STRING; 402612.FP1498; -. DR EnsemblBacteria; CAL43571; CAL43571; FP1498. DR KEGG; fps:FP1498; -. DR PATRIC; fig|402612.5.peg.1512; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_6_1_10; -. DR OrthoDB; 9805987at2; -. DR Proteomes; UP000006394; 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 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; 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..601 FT /note="Arginine--tRNA ligase" FT /id="PRO_1000018027" FT MOTIF 133..143 FT /note="'HIGH' region" SQ SEQUENCE 601 AA; 67873 MW; 6EBFC96C78C39B51 CRC64; MSLQEILNPS IKTAIHQLFD LTIEKIEFQS TRKEFDGDIT MVIFPLLKLI KTPQATPNGA KLNPADLGNK IGNYLVENVA QVEAFNVVSG FLNIVIANDY YINFFNTIKT DAQFGFVSPS EHDKAIMVEY SSPNTNKPLH LGHVRNNLLG YSVAEIIKAS GKKVYKTQII NDRGIHICKS MLAWQKFGHS ETPETSGLKG DKLVGKYYVA FDKAYKVEIA ELMLQGKTEE EAKKQAPIII EAQQMLLDWE AGKPAVMALW KTMNQWVYDG FATTYKNLGV NFDSYYYESN TYLLGKEVVQ IGLDKGVFEK DPDGSVWIDL TQDGLDRKIV LRSDGTAVYM TQDIGTAIQR VKDFSDVGGM VYTVGNEQDY HFRVLFLILK KLGFDWASSL YHLSYGMVEL PSGKMKSREG TVVDADDLME EMTSTAQKLS EDLGKLESYS EEEKAILYKT IGLGALKYYI LKVDPKKSMM FNPEESVDFA GNTGPFIQYT YARIQSILRK ANFDITVTIS TKLHPKEKEL IKQIEMYPEV IQHAAANHSP ALIANYIYDL VKEYNSFYQT VSILGEEDND KKVFRVQLSK KVADTIKTAF TLLGIDVPER M //