ID   SYGA_PASMU              Reviewed;         300 AA.
AC   P57904;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=PM1098;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03182.1; -; Genomic_DNA.
DR   RefSeq; WP_005723293.1; NC_002663.1.
DR   AlphaFoldDB; P57904; -.
DR   SMR; P57904; -.
DR   STRING; 747.DR93_865; -.
DR   EnsemblBacteria; AAK03182; AAK03182; PM1098.
DR   GeneID; 62224971; -.
DR   KEGG; pmu:PM1098; -.
DR   HOGENOM; CLU_057066_1_0_6; -.
DR   OMA; SYYQFQV; -.
DR   Proteomes; UP000000809; 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; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000072853"
SQ   SEQUENCE   300 AA;  34224 MW;  6E2ABCA2B7B9D471 CRC64;
     MTKFNVKTFQ GMILALQDYW ANQGCVIVQP FDMEVGAGTS HPMTCLKALG PEPMAAAYVQ
     PSRRPTDGRY GENPNRLQHY YQFQVVIKPS PDNIQELYLD SLKMLGFDPT QNDIRFVEDN
     WENPTLGAWG LGWEVWLNGM EVTQFTYFQQ VGGLECKPVT GEITYGLERL AMYIQGVDSV
     YDLVWSDGPL GKTTYGDVFH QNEVEQSTYN FEYANTDFLF YCFDQYEKEA SELLALEKPL
     PLPAYERILK AAHSFNLLDA RKAISVTERQ RYILRIRALT KGVAEAYYAS REALGFPGCK