ID I9R8B0_HELPX Unreviewed; 298 AA. AC I9R8B0; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 28-NOV-2012, entry version 3. DE RecName: Full=Glycine--tRNA ligase alpha subunit; DE EC=6.1.1.14; DE AltName: Full=Glycyl-tRNA synthetase alpha subunit; GN Name=glyQ; OS Helicobacter pylori Hp A-4. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=992032; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hp A-4; RA Blanchard T.G., Czinn S.J., McCracken C., Abolude K., Maroo A., RA Santana-Cruz I., Tallon L.J., Ficke F.W.F.; RT "Genome sequence of Helicobacter pylori Hp A-4."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. 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 (By similarity). CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AKOA01000005; EJB41244.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:EC. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro. 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; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. SQ SEQUENCE 298 AA; 34465 MW; A52D4C1E97E97689 CRC64; MQDFSSLLLK LQEYWKDQGC LVIQPYDIPA GAGTFHPATL LRSLDKKPWN VAYVAPSRRP TDGRYGENPN RLGSYYQFQV VIKPSPSNIQ EMYLKSLEVL GINLNEHDIR FVEDNWESPT LGAWGLGWEV WLDGMEVTQF TYFQQVGGIP CSPIPVEITY GLERLAMYVQ KVENILEIEW AKKDNESVRY AQVHLESEYE FSKYHFEIAS VTRLLEMFKN AQAEALHCLE NKLPLPAYDL VMLCSHFFNI LDARKAISVA ERQNYILQIR DLAKGCAVLY KEQEEEREER LKNALTKA //