ID   SYGA_BORA1              Reviewed;         301 AA.
AC   Q2KX74;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Glycyl-tRNA synthetase alpha subunit;
DE            EC=6.1.1.14;
DE   AltName: Full=Glycine--tRNA ligase alpha subunit;
DE            Short=GlyRS;
GN   Name=glyQ; OrderedLocusNames=BAV0709;
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 + glycine + tRNA(Gly) = AMP + diphosphate
CC       + glycyl-tRNA(Gly).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; AM167904; CAJ48315.1; -; Genomic_DNA.
DR   RefSeq; YP_785242.1; -.
DR   GeneID; 6267103; -.
DR   GenomeReviews; AM167904_GR; BAV0709.
DR   KEGG; bav:BAV0709; -.
DR   NMPDR; fig|521.1.peg.2571; -.
DR   HOGENOM; Q2KX74; -.
DR   OMA; Q2KX74; CRRPTDG.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00254; -; 1.
DR   InterPro; IPR006194; Gly-tRNA-synth_II_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_synth_IIc_asu.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   ProDom; PD006985; tRNA_synt_2e; 1.
DR   TIGRFAMs; TIGR00388; glyQ; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    301       Glycyl-tRNA synthetase alpha subunit.
FT                                /FTId=PRO_1000047400.
SQ   SEQUENCE   301 AA;  34307 MW;  5476932C9097CD22 CRC64;
     MLTFQQIILT LQEYWDKQGC ALLQPYDMEV GAGTSHTATF LRAIGPEPWR AAYVQPSRRP
     KDGRYGENPN RLQHYYQYQV VLKPAPPEIL DLYIGSLKAL GIDPAQHDIR FVEDDWENPT
     LGAWGLGWEV WLNGMEVTQF TYFQQVGGLD CTPTTGEITY GLERLAMYLQ NVESVYDLVW
     TEGANGQRVL YRDVFHQNEV EQSTYNFEHS SAEMLFAHFN DYEAEAKRLM EVPLALPAYE
     AALKAAHTFN MLDARGAISV TERAAYIGRI RNLSRAVAQA YYDSRERLGF PMLRNKAGEA
     A
//