ID SYR_WOLSU Reviewed; 528 AA. AC Q7MAK6; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 104. 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=WS0186; OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / OS NCTC 11488 / FDC 602W) (Vibrio succinogenes). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Wolinella. OX NCBI_TaxID=273121; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / RC NCTC 11488 / FDC 602W; RX PubMed=14500908; DOI=10.1073/pnas.1932838100; RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., RA Meyer F., Lederer H., Schuster S.C.; RT "Complete genome sequence and analysis of Wolinella succinogenes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003). 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; BX571657; CAE09347.1; -; Genomic_DNA. DR RefSeq; WP_011138147.1; NC_005090.1. DR AlphaFoldDB; Q7MAK6; -. DR SMR; Q7MAK6; -. DR STRING; 273121.WS0186; -. DR KEGG; wsu:WS0186; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_0_1_7; -. DR Proteomes; UP000000422; 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..528 FT /note="Arginine--tRNA ligase" FT /id="PRO_0000242122" FT MOTIF 112..122 FT /note="'HIGH' region" SQ SEQUENCE 528 AA; 59256 MW; C9136A66832E3FD7 CRC64; MHHTIKHLLE TTLGFSVVLE KPKDKNHGHY ATPAAFSLAK ELKKNPALIA QELSKKLSEI EVFESVQSVG GYINFRLKQG FLDAQASLAL SQGREFGKGD KQGSILLEYV SANPTGPLHI GHARGAVLGD ALSRIGRHLG YALETEYYVN DAGNQIHLLG LSIYLAGRDS LLSLPVTYPE QYYRGEYIVD IAKEALKKWG EKAFADEAFI PELSLFGKEL MLEEIRSNLA DTHIHFDHYV SEKSLYPRWE ETYALLQSHQ GCYEGGGKVW LRSSAHGDEK DRVIVRESGE PTYLAGDIIY HADKFARPYD RYINIWGADH HGYIARVKAA IEFLGHDSSK LEVLLSQMVT LLKGGQPYKM SKRAGNFILM RDVLEDIGAD ALRFIFLSKK PDTHLEFDVD DLNKEDSSNP IFYINYAHAR IHTMLGKSSL DSQEIEAASL EGLEDSIFDL LFLSLQLPQV LEDSFENRAI QKVAEYLRAL AGEFHKFYNE HKILETPQEA ALLKVCKVVA LSLSQGLALL GITAKERM //