ID SYR_XYLF2 Reviewed; 562 AA. AC B2I6M4; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 77. 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=XfasM23_0109; OS Xylella fastidiosa (strain M23). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=405441; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M23; RX PubMed=20601474; DOI=10.1128/jb.00651-10; RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.; RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23) RT causing almond leaf scorch disease in California."; RL J. Bacteriol. 192:4534-4534(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; CP001011; ACB91566.1; -; Genomic_DNA. DR RefSeq; WP_011097507.1; NC_010577.1. DR AlphaFoldDB; B2I6M4; -. DR SMR; B2I6M4; -. DR GeneID; 58015675; -. DR KEGG; xfn:XfasM23_0109; -. DR HOGENOM; CLU_006406_0_1_6; -. DR Proteomes; UP000001698; 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. FT CHAIN 1..562 FT /note="Arginine--tRNA ligase" FT /id="PRO_1000095423" FT MOTIF 129..139 FT /note="'HIGH' region" SQ SEQUENCE 562 AA; 62537 MW; 5857496C60734EE5 CRC64; MKAPVRALIC QGIEALRSNG TLPTNTLPPD FVVERPKTRK HGDFATNVAM LLSKATGSNP RLLAQTLVAA LPTSADIARI EIAGPGFINF HLHPVAYQRE TINVLKQDND YGRNLSGQSR TVGVEYVSAN PTGPLHVGHG RAAAIGDCLA RLLEANGWNV KREFYYNDAG VQIENLVRSV QARARGLKPG DALWPTDAYN GEYIADIAKA YLAGDSINMV DTIITSTKNV DDTAAIHHFA VNYLRNEQNH DLAAFNVDFD IYFLESSLYK DGKVEETVQK LINSGHTYEE GGALWLKSTH FGDDKDRVMR KSDGSYTYFV PDIAYHLSKW QRGYERAITE LGADHHGSLA RVHAGLQALE IGIPPGWPEY VLHQMVTVMR GGEEVKLSKR SGGYVTLRDL IEETSTDATR WFLIARKPDS QLTFDIDLAR QKSNDNPVFY VQYAYARVCS LMHQAHEKNL NYDQTSGMAS LDQLSDNTSL CLMIEISRYP EIVQIACELL EPHLIAQYLR ELAHAFHTWY HNTPVLVENA VERNAKLTLA CATRQVLANG LNLLGVGTPE KM //