ID I9R8B0_HELPX Unreviewed; 298 AA. AC I9R8B0; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 22-FEB-2023, entry version 39. DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254}; DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254}; DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254}; DE Short=GlyRS {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, ECO:0000313|Proteomes:UP000003633}; RN [1] {ECO:0000313|EMBL:EJB41244.1, ECO:0000313|Proteomes:UP000003633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hp A-4 {ECO:0000313|EMBL:EJB41244.1, RC ECO:0000313|Proteomes:UP000003633}; 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 ulcer RT disease, or gastritis."; RL Pathog. Dis. 68:39-43(2013). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl- CC tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA- CC COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215; CC EC=6.1.1.14; Evidence={ECO:0000256|ARBA:ARBA00000201, CC ECO:0000256|HAMAP-Rule:MF_00254}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00254}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00254}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; I9R8B0; -. DR EnsemblBacteria; EJB41244; EJB41244; HPHPA4_1200. DR PATRIC; fig|992032.3.peg.1165; -. DR Proteomes; UP000003633; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00733; GlyRS_alpha_core; 1. DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer. DR InterPro; IPR002310; Gly-tRNA_ligase_asu. DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2; 1. DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1. DR Pfam; PF02091; tRNA-synt_2e; 1. DR PRINTS; PR01044; TRNASYNTHGA. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. 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|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00254}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00254}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00254}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00254}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00254}. 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 //