ID SYR_WOLTR Reviewed; 565 AA. AC Q5GT78; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 110. 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=Wbm0205; OS Wolbachia sp. subsp. Brugia malayi (strain TRS). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=292805; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TRS; RX PubMed=15780005; DOI=10.1371/journal.pbio.0030121; RA Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N., RA Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J., RA Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S., RA Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D., RA Koonin E., Slatko B.; RT "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a RT human pathogenic nematode."; RL PLoS Biol. 3:599-614(2005). 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; AE017321; AAW70796.1; -; Genomic_DNA. DR RefSeq; WP_011256406.1; NC_006833.1. DR AlphaFoldDB; Q5GT78; -. DR SMR; Q5GT78; -. DR STRING; 292805.Wbm0205; -. DR KEGG; wbm:Wbm0205; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_0_1_5; -. DR Proteomes; UP000000534; 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; Reference proteome. FT CHAIN 1..565 FT /note="Arginine--tRNA ligase" FT /id="PRO_0000242121" FT MOTIF 126..136 FT /note="'HIGH' region" SQ SEQUENCE 565 AA; 64200 MW; CD7307E0A40995E5 CRC64; MNIFKRISSL ILSKLDKLKQ GVSSVTNFIV EPPSNRAHGD IYTNIAMVLA KHEKKKPVEI AEVLAKEFAL FDEIARVEIA GPGFINMHLK IEVWHGILEQ INELKTEFGT LNIGNNQAIN VEFVSANPTG PLHIGHARGA VFGDVLTNLL KKVGYRVTKE YYINDAGAQI DTLVRSVYLR YKEALGEKIS IEKGLYPGEY LKPIGEELAK KYGRELLEKQ DNRVIREYTL SSILELIKEG MNLLGVSHDV FTSEYELQKS GKIEKSIKLL SDKGLVYEGY LEKPKSKESE NWTSRKEMLF RSTEFGDDVD RALKKEDGSW TYFASDIAYH FDKISRGFNN MIVALGSDHG GYIKRLKAVI SALSDNQAKI EVKLHNVVNF FENGKPVKMS KRSGNFLTVR DVVEEVGRDI TRFIMLTRKN DMVLDFDFTK VKEQSKDNPI FYVQYAHVRA HSLMRNAPKE LPKANPSLLK TNGELFLIKT LAKWPDVVET AARLCEPHRI TFYLLEVAEA FHILWGYGKS DLNMRFILED NPNLTAARMF LVQALVHVIA SGLSMFNIEP LEEMK //