ID   SYGA_HELPJ              Reviewed;         298 AA.
AC   Q9ZKP1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit;
DE            EC=6.1.1.14;
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit;
DE            Short=GlyRS;
GN   Name=glyQ; OrderedLocusNames=jhp_0894;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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;
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AE001439; AAD06462.1; -; Genomic_DNA.
DR   PIR; G71876; G71876.
DR   RefSeq; WP_001150875.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZKP1; -.
DR   SMR; Q9ZKP1; -.
DR   STRING; 85963.jhp_0894; -.
DR   EnsemblBacteria; AAD06462; AAD06462; jhp_0894.
DR   KEGG; hpj:jhp_0894; -.
DR   PATRIC; fig|85963.30.peg.67; -.
DR   eggNOG; COG0752; Bacteria.
DR   OMA; SYYQFQV; -.
DR   Proteomes; UP000000804; Chromosome.
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   Gene3D; 3.30.930.10; -; 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   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   SUPFAM; SSF55681; SSF55681; 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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..298
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000072843"
SQ   SEQUENCE   298 AA;  34491 MW;  1416323B3E184278 CRC64;
     MQDFSSLLLK LQEYWKDQGC LVIQPYDIPA GAGTFHPATL LRSLDKKPWN VAYVAPSRRP
     TDGRYGENPN RLGSYYQFQV VIKPSPSNIQ ELYLKSLEVL GINLNEHDIR FVEDNWESPT
     LGAWGLGWEV WLDGMEVTQF TYFQQVGGIP CSPIPVEITY GLERLTMYVQ KVENILEIEW
     AKKDNESVRY AQVHLESEYE FSKYHFEVAS VERLLEMFKN AQAEALHCLE NKLPLPAYDL
     VMLCSHFFNI LDARKAISVA ERQNYILQIR DLAKGCAVLY KEQEEEREER LKNALTKA