(data stored in ACNUC7421 zone)

SWISSPROT: SYGA_PSEAB

ID   SYGA_PSEAB              Reviewed;         315 AA.
AC   Q02V72;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 61.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000255|HAMAP-Rule:MF_00254};
GN   OrderedLocusNames=PA14_00100;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
CC       + glycyl-tRNA(Gly). {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00254}.
DR   EMBL; CP000438; ABJ14965.1; -; Genomic_DNA.
DR   RefSeq; WP_003097276.1; NC_008463.1.
DR   ProteinModelPortal; Q02V72; -.
DR   SMR; Q02V72; -.
DR   EnsemblBacteria; ABJ14965; ABJ14965; PA14_00100.
DR   KEGG; pau:PA14_00100; -.
DR   HOGENOM; HOG000264291; -.
DR   KO; K01878; -.
DR   OMA; LGSYYQF; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00733; GlyRS_alpha_core; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   TIGRFAMs; TIGR00388; glyQ; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02V72.
DR   SWISS-2DPAGE; Q02V72.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    315       Glycine--tRNA ligase alpha subunit.
FT                                /FTId=PRO_1000047468.
SQ   SEQUENCE   315 AA;  36141 MW;  C13AB05877BAD116 CRC64;
     MSQTTPAVRT FQDLILALQN YWAEQGCVVL QPYDMEVGAG TFHTATFLRA IGPETWNAAY
     VQPSRRPTDG RYGENPNRLQ HYYQFQVVLK PNPENFQELY LGSLKAIGID PLVHDIRFVE
     DNWESPTLGA WGLGWEIWLN GMEVTQFTYF QQVGGIECYP VTGEITYGLE RLAMYLQGVD
     SVYDLVWTDG PFGKVTYGDV FHQNEVEQST FNFEHANVPK LFELFDFYES EANRLIALEL
     PLPTYEMVLK ASHTFNLLDA RRAISVTERQ RYILRVRTLA RAVAQSYLQA RARLGFPMAT
     PELRDEVLAK LKEAE
//

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