ID   SYR_BUCBP               Reviewed;         578 AA.
AC   P59483;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=bbp_224;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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; AE016826; AAO26955.1; -; Genomic_DNA.
DR   RefSeq; WP_011091356.1; NC_004545.1.
DR   AlphaFoldDB; P59483; -.
DR   SMR; P59483; -.
DR   STRING; 224915.bbp_224; -.
DR   EnsemblBacteria; AAO26955; AAO26955; bbp_224.
DR   GeneID; 56470766; -.
DR   KEGG; bab:bbp_224; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_6; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000000601; 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   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; 1.
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..578
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151541"
FT   MOTIF           125..135
FT                   /note="'HIGH' region"
SQ   SEQUENCE   578 AA;  67542 MW;  FF6F76245F6D1AB4 CRC64;
     MTIKSIISKH IKKVLNIIKI FITHEDLAIV RTSDKKVWDY QVNGIIKLAN NLNKNPYVLS
     KYIISNMRYY EYKMYKKITA SKLGFINIFI NKTWLEKELT KKIKSFRLGI KKVTPKNIII
     DYSSPNVAKK MHVGHLRSTI LGDATARILE FLGHNVMRIN HIGDWGTHFG MIIAYLKQNF
     ISYNEINQLD LNELYQKAKV NFDLDSEFSK KTRNYVVKLQ KKDKECIRIW KKIVKKTITE
     NQKIYKKLNV TLTNKHIVGE SFYNDMLPDI IQDLKTKKIA KQCNGAYIVF LNKFKNRDGA
     PMGVIIQKQD GAFLYSTIDL ACLKYRCEVL RADQILYFID SRQKEYLKQI LEIAKKAGYI
     SNNIIIRHNE FGMICSKNKR PFSTRSGNNI ILSDLINEAI KRAKKIAKNK NKNLSNKELE
     YLSEKIGIGA IKYFDLSKNR LTDYIFKWDE ILTFDGNTAP YMQYAYIRIL SIFKKLNISM
     LKLSGNIILT ELLENKLAIK LFQFEEIILE SLQHSAPHII CKYLYELSKI FSKFYEKCSI
     YKSKNTKIRK NRLLLSLLTA RTLKKGLFII GISTIKYM