ID   SYR_RHIE6               Reviewed;         585 AA.
AC   B3PXT5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   10-JUN-2026, entry version 85.
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=RHECIAT_CH0001904;
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652;
RX   PubMed=20048063; DOI=10.1128/aem.02039-09;
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P., Fernandez J.L.,
RA   Hernandez Gonzalez I.L., Diaz R., Flores M., Palacios R., Mora J.,
RA   Davila G.;
RT   "Conserved symbiotic plasmid DNA sequences in the multireplicon pangenomic
RT   structure of Rhizobium etli.";
RL   Appl. Environ. Microbiol. 76:1604-1614(2010).
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; CP001074; ACE90871.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3PXT5; -.
DR   SMR; B3PXT5; -.
DR   KEGG; rec:RHECIAT_CH0001904; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_5; -.
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   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; 2.
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..585
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000095396"
FT   MOTIF           131..141
FT                   /note="'HIGH' region"
SQ   SEQUENCE   585 AA;  64715 MW;  27303118B5652650 CRC64;
     MNLFTDFEAR IKTALEQIDL VREKRSELDF GRITVEPPRD ASHGDVATNA AMVLAKPLGS
     NPRALADVII AKLKEDADVA DVSVAGPGFI NIRLSVGYWQ RLLASMINSG TDYGRSTLGA
     GRKVNVEYVS ANPTGPMHVG HCRGAVVGDA LANLLAFAGY GVEKEYYIND AGSQIDVLAR
     SVFLRYREAL GERIGEIPSG LYPGDYLVPV GQSLAADYGV RLHNMPEEQW MPIVKDRTIS
     AMMVMIREDL AALNVHHDIF FSERTLHANG AAAIRTAIND LTFKGYVYKG TLPPPKGQLP
     EDWEDREQTL FRSTEVGDDM DRPLIKSDGS YTYFAADVAY FKNKFDRGFD EMIYVLGADH
     GGYVKRLEAV ARGVSNGKAK LTVLLCQLVK LYRNGEPVKM SKRSGDFVTL RDVVEEVGRD
     SVRFMMLYRK NSEPLDFDFA KVTEQSKDNP VFYVQYAHAR CMSVFRQARE AFPGLEVSAE
     DLAKAVAGIG DPAELQLVAK LAEFPRVVEA AAQSQEPHRI AFYLYDLASS FHAHWNKGKD
     QTELRFVNDK NRESSIARLG LVYAVASVLK SGLAITGTAA PDEMR
//