ID   SYR_BUCAP               Reviewed;         580 AA.
AC   Q08888;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   Name=argS; OrderedLocusNames=BUsg_237;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131.
RX   PubMed=7507875; DOI=10.1016/0378-1119(93)90003-l;
RA   Munson M.A., Baumann L., Baumann P.;
RT   "Buchnera aphidicola (a prokaryotic endosymbiont of aphids) contains a
RT   putative 16S rRNA operon unlinked to the 23S rRNA-encoding gene: sequence
RT   determination, and promoter and terminator analysis.";
RL   Gene 137:171-178(1993).
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;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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; AE013218; AAM67796.1; -; Genomic_DNA.
DR   EMBL; L18927; AAA17432.1; -; Genomic_DNA.
DR   PIR; I40591; I40591.
DR   RefSeq; WP_011053763.1; NC_004061.1.
DR   AlphaFoldDB; Q08888; -.
DR   SMR; Q08888; -.
DR   STRING; 198804.BUsg_237; -.
DR   GeneID; 75258888; -.
DR   KEGG; bas:BUsg_237; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_6; -.
DR   Proteomes; UP000000416; 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; cd07956; Anticodon_Ia_Arg; 1.
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.
FT   CHAIN           1..580
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151540"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   580 AA;  68043 MW;  CFE972DC5DC43ED5 CRC64;
     MNIKYLIKKD IEQALIKINS NYTYEVFIIS SKKIELGHYQ VDNLMKISSR LKIKPYKLFQ
     KILILIEKKK IYKKIIFSHP GFINIFIKNE WLSEKLEIPF ISSRLGVKYI YPKKNIVIDY
     SSPNIAKEMH VGHLRSTIIG DVTVRILEFL GQKVIRANHI GDWGTQFGIL IAYLEDKKLL
     KKLKKNLLSL QDLDNIYCQS KKQYNSNELF SKKSREFVVK LQNGDQYCCA IWKKLVSITM
     LENYKIYKKL NVTLEEKHTM GESFYNPMLP KIVEDLKKQK IAIEKNGAVI VFLDEFKNRM
     GDSMGVIIRK KDKGFLYSTT DIACLKYRYQ NLHADRIIYY TDSRQYQHLL QSWTIAEKAN
     YISKNLLLEH HMFGMMLSKN RRPFKTRDGN TIKLSNLLNE SINRATNLIQ KKQPNLCKKK
     LIKLGEIIGI SAVKYSDLSK NRNTNYIFDW DKMLSFEGNT APYIQYAYTR IISILKKSNI
     PLHKIKMKII LNEESEINLA IKILEFEEII LLIAKNGTPH IMCKYLYQLS TYFSHFYENC
     SILFSEKIKI RKSRIKLSFL TAKTIKKGLN LLGIKTIKKM
//