ID   SYR_CAUVN               Reviewed;         600 AA.
AC   B8H4W0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=CCNA_03469;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(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}.
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DR   EMBL; CP001340; ACL96934.1; -; Genomic_DNA.
DR   RefSeq; WP_010921188.1; NC_011916.1.
DR   RefSeq; YP_002518842.1; NC_011916.1.
DR   AlphaFoldDB; B8H4W0; -.
DR   SMR; B8H4W0; -.
DR   PRIDE; B8H4W0; -.
DR   EnsemblBacteria; ACL96934; ACL96934; CCNA_03469.
DR   GeneID; 7332466; -.
DR   KEGG; ccs:CCNA_03469; -.
DR   PATRIC; fig|565050.3.peg.3383; -.
DR   HOGENOM; CLU_006406_5_1_5; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   PhylomeDB; B8H4W0; -.
DR   Proteomes; UP000001364; 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; -; 1.
DR   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR11956; PTHR11956; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 2.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   TIGRFAMs; TIGR00456; argS; 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..600
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000198882"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   600 AA;  66335 MW;  AEACF49AE89F5D21 CRC64;
     MNDLKRSLSE AAAAAFQAAG LPPEFGRVTA SDRPDLADFQ CNGALAAAKS AKRNPREIAV
     QVVDILKGDP RLASVEIAGV GFINMRVSDE ALSARAREIA SDDRTGAQLL ETPRRVLIDY
     AGPNVAKPMH VGHLRASIIG ESVKRLYRFR GDDVVGDAHF GDWGFQMGLL ISAIMDEDPF
     INALMEKLPE APRGFSSADE AKVMAEFEKR ITLADLDRIY PAASVRQKED PAFKERARKA
     TAELQNGRFG YRLLWRHFVN VSRVALEREF HALGVDFDLW KGESDVNDLI EPMVLQLEAK
     GLLVQDQGAR IVRVAREGDK RDVPPLLVVS SEGSAMYGTT DLATILDRRK SFDPHLILYC
     VDQRQADHFE TVFRAAYLAG YAEEGALEHI GFGTMNGADG KPFKTRAGGV LKLHDLIEMA
     REKARERLRE AGLGAELSEE QFEDTAHKVG VAALKFADLQ NFRGTSYVFD LDRFTSFEGK
     TGPYLLYQSV RIKSVLRRAA ESGAVAGRVE IHEPAERDLA MLLDAFEGAL QEAYDKKAPN
     FVAEHAYKLA QSFSKFYAAC PIMSADTETL RASRLTLAET TLRQLELALD LLGIEAPERM