ID SYGA_HAEI8 Reviewed; 302 AA. AC Q4QLY1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 22. 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=NTHI1098; OS Haemophilus influenzae (strain 86-028NP). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=281310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005; RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., RA Munson R.S. Jr.; RT "Genomic sequence of an otitis media isolate of nontypeable RT Haemophilus influenzae: comparative study with H. influenzae serotype RT d, strain KW20."; RL J. Bacteriol. 187:4627-4636(2005). 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. 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; CP000057; AAX87966.1; -; Genomic_DNA. DR RefSeq; YP_248626.1; -. DR GeneID; 3430391; -. DR GenomeReviews; CP000057_GR; NTHI1098. DR KEGG; hit:NTHI1098; -. DR HOGENOM; Q4QLY1; -. DR OMA; Q4QLY1; CRRPTDG. DR BioCyc; HINF281310:NTHI1098-MON; -. 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 1 302 Glycyl-tRNA synthetase alpha subunit. FT /FTId=PRO_1000047427. SQ SEQUENCE 302 AA; 34471 MW; 9FCD91C52A926ABB CRC64; MSTKFNVKTF QGMILALQEY WANQGCTIVQ PFDMEVGAGT SHPMTALRAL GPEPMAFAYV QPSRRPTDGR YGENPNRLQH YYQFQVVIKP SPDNIQELYL GSLEMLGFDP TQNDIRFVED NWENPTLGAW GLGWEVWLNG MEVTQFTYFQ QVGGLECKPV TGEVTYGLER LAMYIQGVDS VYDLVWSDGP LGKTTYGDVF HQNEVEQSTY NFEHANTDFL FYCFDQYEKE AQELLALEKP LPLPAYERIL KAAHSFNLLD ARKAISVTER QRYILRIRAL TKGVAEAYYA SREALGFPGC KK //