ID   SYGA_SYNS9              Reviewed;         290 AA.
AC   Q3AWZ4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   28-JAN-2026, entry version 106.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000255|HAMAP-Rule:MF_00254};
GN   OrderedLocusNames=Syncc9902_1561;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Gly) + glycine + ATP = glycyl-tRNA(Gly) + AMP +
CC         diphosphate; 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:0000255|HAMAP-Rule:MF_00254};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
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DR   EMBL; CP000097; ABB26519.1; -; Genomic_DNA.
DR   RefSeq; WP_011360337.1; NC_007513.1.
DR   AlphaFoldDB; Q3AWZ4; -.
DR   SMR; Q3AWZ4; -.
DR   STRING; 316279.Syncc9902_1561; -.
DR   KEGG; sye:Syncc9902_1561; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_3; -.
DR   OrthoDB; 9802183at2; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   FunFam; 3.30.930.10:FF:000006; Glycine--tRNA ligase alpha subunit; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1.
DR   Gene3D; 1.20.58.180; Class II aaRS and biotin synthetases, domain 2; 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   NCBIfam; TIGR00388; glyQ; 1.
DR   NCBIfam; NF006827; PRK09348.1; 1.
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   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..290
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000047519"
SQ   SEQUENCE   290 AA;  32902 MW;  0219585196BEA87E CRC64;
     MHFQDIIGTL NSFWANQGCL LLQPYDTEKG AGTMSPHTVL RAIGPEPWAV AYPEPCRRPT
     DGRYGDNPNR AQHYFQYQVL IKPSPDAIQE TYLASLEALG IKAADHDIRF VEDNWESPTL
     GAWGVGWEVW LDGMEVTQFT YFQQCGGLDC KPVSIEITYG LERLAMYLQD VESIWDLSWN
     ADRKYGDIWL PFEKGQCKFN FEASNPDRLK QLFAIYEAEA SDLIHQQLPA PALDFVLKCS
     HTFNLLEARG VISVTERTAT IGRIRNLARK VAEAWLVERE ALGFPLLPSN
//