ID   SYR_BUCAI               Reviewed;         574 AA.
AC   Q44683;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 138.
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=BU242;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-158.
RA   Unterman B.M., Baumann P.;
RT   "Partial characterization of the ribosomal RNA operons of the pea aphid
RT   endosymbionts: evolution and physiological implications.";
RL   (In) Campbell R.K., Eikenbary R.D. (eds.);
RL   Aphid-plant genotype interactions, pp.329-350, Elsevier, Amsterdam (1990).
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}.
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DR   EMBL; BA000003; BAB12957.1; -; Genomic_DNA.
DR   EMBL; L18933; AAA72384.1; -; Genomic_DNA.
DR   RefSeq; NP_240071.1; NC_002528.1.
DR   RefSeq; WP_009874199.1; NC_002528.1.
DR   AlphaFoldDB; Q44683; -.
DR   SMR; Q44683; -.
DR   STRING; 563178.BUAP5A_238; -.
DR   EnsemblBacteria; BAB12957; BAB12957; BAB12957.
DR   KEGG; buc:BU242; -.
DR   PATRIC; fig|107806.10.peg.255; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_6; -.
DR   Proteomes; UP000001806; 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; Reference proteome.
FT   CHAIN           1..574
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151539"
FT   MOTIF           121..131
FT                   /note="'HIGH' region"
FT   CONFLICT        9
FT                   /note="E -> K (in Ref. 2; AAA72384)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   574 AA;  66686 MW;  7916BD29FCAB02C1 CRC64;
     MNLKNTIKED IQDALIKIAI INCDPVITLN KKTKIGHYQL NNLIKIANIS NLKPFELANR
     IILNIKKKYM YKEITFSQPG FINFLINPYW ISEQLEKIFL SPRLGINHVN AQNIVIDYSS
     PNIAKEMHIG HLRSTIIGDV MARILDFLGH NVIRANHIGD WGTQFGMLIA YLEVKKLVNS
     PLSLMKLEEY YCKAKKKYDI DQLFAEKSRE YVVKLQNGDQ YCYSIWKKLV SITMLENCKI
     YKRLHVTLKK KHTMGESIYN KMLPNIIEDL KNKKIAIEKN GSTIVFLKEF KNRLGEPMGV
     VIQKKDKGFL YSTTDIACLK YRYQVLHADR IIYYTDSRQH QHLLQAWTIA KKALYISQNL
     LLEHHIFGMM LSKDKRPFKT RDGDTIKLSA LLDEATERAM RLIKNKQPNL SKKKLNQLSN
     IIGVGAVKYA DLSKNRNTNY IFDWNEMLSF EGNTAPYIQY AYTRIVSILK KSNMPIKKLK
     EKIFLTKESE INLAIKILEF EEIILLISQK GTPHILCKYL YHLATSFSHF YENCSILFPK
     KIKTCKSRLK LSILTAKTLK KGLNMLGIRV VKKM
//