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   16-JUN-2009, entry version 69.
DE   RecName: Full=Arginyl-tRNA synthetase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginine--tRNA ligase;
DE            Short=ArgRS;
GN   Name=argS; OrderedLocusNames=BU242;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum
OS   symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=118099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tokyo 1998;
RX   MEDLINE=20445173; 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
RT   Buchnera 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
RT   aphid endosymbionts: evolution and physiological implications.";
RL   (In) Campbell R.K., Eikenbary R.D. (eds.);
RL   Aphid-plant genotype interactions, pp.329-350, Elsevier, Amsterdam
RL   (1990).
CC   -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC       diphosphate + L-arginyl-tRNA(Arg).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; BA000003; BAB12957.1; -; Genomic_DNA.
DR   EMBL; L18933; AAA72384.1; -; Genomic_DNA.
DR   RefSeq; NP_240071.1; -.
DR   HSSP; Q93RP5; 1IQ0.
DR   GeneID; 1109685; -.
DR   GenomeReviews; BA000003_GR; BU242.
DR   KEGG; buc:BU242; -.
DR   HOGENOM; Q44683; -.
DR   OMA; Q44683; YNDDLQP.
DR   BioCyc; BSP107806:BU242-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00123; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-synth_Ic.
DR   InterPro; IPR015945; Arg-tRNA-synth_Ic_core.
DR   InterPro; IPR005148; Arg-tRNA-synth_Ic_N.
DR   InterPro; IPR008909; DALR_anticod_bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11956; Arg_tRNA-synt_1c; 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   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    574       Arginyl-tRNA synthetase.
FT                                /FTId=PRO_0000151539.
FT   MOTIF       121    131       "HIGH" region.
FT   CONFLICT      9      9       E -> K (in Ref. 2; AAA72384).
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
//