ID   SYR_BAUCH               Reviewed;         578 AA.
AC   Q1LTI8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=BCI_0276;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(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; CP000238; ABF13938.1; -; Genomic_DNA.
DR   RefSeq; YP_588726.1; -.
DR   GeneID; 4056684; -.
DR   GenomeReviews; CP000238_GR; BCI_0276.
DR   KEGG; bci:BCI_0276; -.
DR   HOGENOM; Q1LTI8; -.
DR   OMA; Q1LTI8; HMGFGTM.
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    578       Arginyl-tRNA synthetase.
FT                                /FTId=PRO_1000017990.
FT   MOTIF       123    133       "HIGH" region.
SQ   SEQUENCE   578 AA;  65685 MW;  40F42DA61DD484DD CRC64;
     MNIHAIISDQ IHKAMLAAGV PPYYRVQVRP SVKKKFGDYQ INGLMATAKQ LGVPSYFLAK
     KVVSFLQLNG IARQIDIAGP GFINIYLDSQ WLATKIATAI ASPRLGISLI ELPQTIVVDY
     SSPNIAKEMH VGHIRSTIIG DASARILDFI GHKVIRINHI GDWGTHFGML IAYLQQVEKN
     IDPEIPLSFL DQLYRQAKDK YDTDPSFAQE ARNCVVKLQC GDSFCLKIWQ KLVKITINEN
     QKIYNRLNIS LSHENIMGES KYNNMLPNII ADLKAKGLAV ESAGATVIFL NEFQDKQGNP
     LGVIIQKKDG AYLYTTTDIA CIKYRYEQLK ADRIIYYVDS RQHQHLKQIW TIVRKAGYIP
     QTMQLDHHMF GMIFDKEGKP FKTRVGVNIK LNDLLDEALK RARCLILSKN MDVDPVELEH
     LAQVISISAI KYAELSKNRT TDYIFNWDDM LSFEGNTAPY ILYAYTRIAS ILKRSNYNKQ
     QILTGSILLE KEHEHLLAVR LLQYHETITT VAHDGRPHIL CGYLYNLAVR FSSFYEHCSI
     INANSDIQRK SRLQLALLTS KTLQHGLSLL GIETVDKM
//