ID   SYGA_BUCAI              Reviewed;         312 AA.
AC   P57236;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=BU136;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB12854.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000003; BAB12854.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_239968.2; NC_002528.1.
DR   RefSeq; WP_009874092.1; NC_002528.1.
DR   AlphaFoldDB; P57236; -.
DR   SMR; P57236; -.
DR   STRING; 107806.10038819; -.
DR   EnsemblBacteria; BAB12854; BAB12854; BAB12854.
DR   KEGG; buc:BU136; -.
DR   PATRIC; fig|107806.10.peg.145; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_6; -.
DR   OMA; SYYQFQV; -.
DR   Proteomes; UP000001806; 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   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..312
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000072830"
SQ   SEQUENCE   312 AA;  36961 MW;  A138A9BEBC6CE8C6 CRC64;
     MKNYHNNFHK LITILQEYWL QQGCTIFQPL DLPIGAGTFH NITFLGTIGP EPINAAYIQS
     CRRPSDGRYG ENPNRLQHYY QFQVIIKPPP NNIQNIYLNS LYLLNIDEKI HDIRFVEDNW
     ENPTLGAWGI GWEVWLNGME ITQFTYFQQV GGLECKPVSV EITYGLERIA MHMQNKSNVY
     DLIWNEYNHK KITYGDIFQQ NEREQSQYNF QYSDVNFLFD CFKKYELEAK KLINLKEPLL
     LVSYEKILQA NHIFNLLDAR KSLSSNERQS YILRIRKLTS QVAIKYLNLR KNLGFPLCHK
     KREIHDKENI IN