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   16-JUN-2009, entry version 72.
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=BUsg_237;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; 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   MEDLINE=94131280; 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:
RT   sequence determination, and promoter and terminator analysis.";
RL   Gene 137:171-178(1993).
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; AE013218; AAM67796.1; -; Genomic_DNA.
DR   EMBL; L18927; AAA17432.1; -; Genomic_DNA.
DR   PIR; I40591; I40591.
DR   RefSeq; NP_660585.1; -.
DR   GeneID; 1005438; -.
DR   GenomeReviews; AE013218_GR; BUsg_237.
DR   KEGG; bas:BUsg237; -.
DR   HOGENOM; Q08888; -.
DR   OMA; Q08888; HMGFGTM.
DR   BioCyc; BAPH198804:BUSG237-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    580       Arginyl-tRNA synthetase.
FT                                /FTId=PRO_0000151540.
FT   MOTIF       123    133       "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
//