ID   SYR_CUPTR               Reviewed;         595 AA.
AC   B2AG76;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   28-JAN-2026, entry version 94.
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=RALTA_A0102;
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1;
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Arg) + L-arginine + ATP = L-arginyl-tRNA(Arg) + AMP +
CC         diphosphate; 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; CU633749; CAP62775.1; -; Genomic_DNA.
DR   RefSeq; WP_012351443.1; NC_010528.1.
DR   AlphaFoldDB; B2AG76; -.
DR   SMR; B2AG76; -.
DR   GeneID; 29762022; -.
DR   KEGG; cti:RALTA_A0102; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_4; -.
DR   BioCyc; CTAI977880:RALTA_RS00505-MONOMER; -.
DR   Proteomes; UP000001692; Chromosome 1.
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   FunFam; 1.10.730.10:FF:000008; Arginine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000062; Arginine--tRNA ligase; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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; 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..595
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000095356"
FT   MOTIF           132..142
FT                   /note="'HIGH' region"
SQ   SEQUENCE   595 AA;  64609 MW;  5A03CE879A7E52B5 CRC64;
     MLPVQTSNLA AAFTDAVRAL APADATLPAV TFERPKVAAH GDLACNVAMQ VARALKSNPR
     ELAQRIVAAV EADARAQGLV AGMDIAGPGF INLRLTPSAK ADVLRAVLNE GDHYGARERG
     VHGQVLVEFV SANPTGPLHV GHGRQAALGD ALANLLSWQG WHVHREFYYN DAGVQIQTLA
     LSVQARARGL KPGDASWPEA AYNGDYIADI AADFLAGKTV SASDGEPVTA SGNVEDIDSI
     RKFAVTYLRN EQDIDLQAFG VKFDRYYLES SLYSDGRVDA AVQSLIDKGK TYESEGALWL
     RTTDDGDDKD RVMKKSDGTY TYFVPDVAYH TTKWERGFTK VINVQGSDHH GTIARVRAGL
     QGLDIGIPQG YPDYVLHKMV TVMKNGEEVK ISKRAGSYVT VRDLIEWSNG GDETIRGCLE
     QGVADWPAHF TRGRDAVRFF LLSRKADTEF VFDVDLALKQ NDENPVYYVQ YAHARICSIF
     ESWGGADWES RLAELAGADL SAVTGADASA QALALGRRLA EFPDMLAAAA AELAPHAVAF
     YLRDLAGDFH AFYNADRVLV DDEAVKRARL ALLAATRQVL RNGLAVIGVS APRRM
//