ID   SYR_BORA1               Reviewed;         561 AA.
AC   Q2KTN9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=BAV3361;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AM167904; CAJ50971.1; -; Genomic_DNA.
DR   RefSeq; YP_787856.1; -.
DR   GeneID; 6266525; -.
DR   GenomeReviews; AM167904_GR; BAV3361.
DR   KEGG; bav:BAV3361; -.
DR   NMPDR; fig|521.1.peg.1913; -.
DR   HOGENOM; Q2KTN9; -.
DR   OMA; Q2KTN9; ADHHGYV.
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:3.30.1360.70; Arg-tRNA-synth_Ic_N; 1.
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    561       Arginyl-tRNA synthetase.
FT                                /FTId=PRO_0000241992.
FT   MOTIF       129    139       "HIGH" region.
SQ   SEQUENCE   561 AA;  61604 MW;  B606CF5844884694 CRC64;
     MLPEQQQHLI SLLARAVAGI LPEASPDILL ERPKVAAHGD VATNVAMQLA KPAKRNPREL
     AQGIVDALLA DPQARAIVDS AEIAGPGFIN LRFTAQARQA VVAAVSAQGA AFGRAARRDE
     KVLVEFVSAN PTGPLHVGHA RQAALGDAIC RLFDASGWDV TREFYYNDAG NQIQNLAISV
     QARARGIGPD APEWPADGYK GDYIADIARD YLAQASVQAA DGEPVQASGN IDDLEDIRAF
     AVAYLRREQD LDLQAFGLKF DNFFLESSLY TSGRVERTVE TLIAKGHTYE QDGALWLRTT
     ELGTGDDKDR VMRKSEGGYT YFVPDVAYHL AKWERGFHHA INIQGSDHHG TVARVRAGLQ
     GLEEGIPKEF PAYVLHKMVK VMRGGEEVKI SKRAGSYVTM RDLIEWVGRD AVRYFLIQRR
     ADTEFVFDID LALSKSDENP VYYIQYAHAR ICSMIASSGL DDATIAAADA ARLTAPSEFA
     LMQRLAEFPN VVKLAAQELA PHHIAFWLRD CASDFHGWYN AERVLVDDEG LKQARLRLAA
     TTRQVLANGL ALLGVTALER M
//