ID   SYR_BUCCC               Reviewed;         571 AA.
AC   Q057S1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
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=BCc_152;
OS   Buchnera aphidicola subsp. Cinara cedri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=372461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17038625; DOI=10.1126/science.1130441;
RA   Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M.,
RA   Michelena J.M., Silva F.J., Moya A., Latorre A.;
RT   "A small microbial genome: the end of a long symbiotic relationship?";
RL   Science 314:312-313(2006).
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; CP000263; ABJ90628.1; -; Genomic_DNA.
DR   RefSeq; YP_802721.1; -.
DR   GeneID; 4440620; -.
DR   GenomeReviews; CP000263_GR; BCc_152.
DR   KEGG; bcc:BCc_152; -.
DR   OMA; Q057S1; YNDDLQP.
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    571       Arginyl-tRNA synthetase.
FT                                /FTId=PRO_1000017996.
FT   MOTIF       122    132       "HIGH" region.
SQ   SEQUENCE   571 AA;  67427 MW;  C6AFCC0856C9BEB5 CRC64;
     MNIQKFLKKK IKKICIKLGL PENFNPIIQK NIKKKNIDYQ INGIIKLKKK KSNYHYKLAK
     KISYYMNKSK IYKKISISKP GFINITLDSN WICTNINNMF IAKNFNISFK KPKKIIIDYS
     SPNIAKEMHV GHLRSTILGD TTARILKFLG HNVIKQNHIG DWGIQFGMLI TQLKLESKIS
     FKNIEKIYKK SYLNYKKNPI FFKKTKKNVV KLQKKDKKCI YIWKKIVKKS IKKNNKVYKK
     LNVSLKKKDI RGESFYNFML PGIISDLKKK KIAVNYQGCV IVYLKNFKNR LGKKMGVVIQ
     KKDGAFLYTT TDIACLKYRC KTLKADRIIY YIDNRQKQHL LQIWNIAKKA KYFTKKILLE
     HHSFGMILHK NKKPFKTRNG DTIKLIKLLN KGVTKAKEKI KKKNRKIKKK ELKKIAHNIG
     IGAIKYFDLS KKRKLDYIFD WDKMLSLEGN TAPYIQYAYI RIKSIIKKNT TIFQNDKYKI
     NIFTSFERQL IFSIFQFEEI IHILEKKGTP HLMCNYLYDL SGKFSKFYEN CSILNAKEKH
     IKISRIKLSI LTSKIIKKCL YFLGIKTVSK M
//