ID I9R8B0_HELPX Unreviewed; 298 AA. AC I9R8B0; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 24-JUN-2015, entry version 15. DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254, ECO:0000256|SAAS:SAAS00104892}; DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254, ECO:0000256|SAAS:SAAS00104898}; DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254}; GN Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254, GN ECO:0000313|EMBL:EJB41244.1}; GN ORFNames=HPHPA4_1200 {ECO:0000313|EMBL:EJB41244.1}; OS Helicobacter pylori Hp A-4. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=992032 {ECO:0000313|EMBL:EJB41244.1}; RN [1] {ECO:0000313|EMBL:EJB41244.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hp A-4 {ECO:0000313|EMBL:EJB41244.1}; RX PubMed=23661595; DOI=10.1111/2049-632X.12045; RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M., RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K., RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.; RT "Genome sequences of 65 Helicobacter pylori strains isolated from RT asymptomatic individuals and patients with gastric cancer, peptic RT ulcer disease, or gastritis."; RL Pathogens Dis 68:39-43(2013). CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). {ECO:0000256|HAMAP-Rule:MF_00254, CC ECO:0000256|SAAS:SAAS00104881}. CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000256|HAMAP-Rule:MF_00254, ECO:0000256|SAAS:SAAS00104875}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254, CC ECO:0000256|SAAS:SAAS00104849}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000256|HAMAP-Rule:MF_00254}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJB41244.1}. 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 RefSeq; WP_001150887.1; NZ_AKOA01000005.1. DR EnsemblBacteria; EJB41244; EJB41244; HPHPA4_1200. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. 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 {ECO:0000256|HAMAP-Rule:MF_00254, KW ECO:0000256|SAAS:SAAS00104890}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00254, KW ECO:0000256|SAAS:SAAS00104871}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254, KW ECO:0000256|SAAS:SAAS00104901}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00254, KW ECO:0000256|SAAS:SAAS00104859}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00254, KW ECO:0000256|SAAS:SAAS00104858}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00254, KW ECO:0000256|SAAS:SAAS00104852}. 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 //