ID   SYGA_TRIEI              Reviewed;         294 AA.
AC   Q10XW9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
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}; OrderedLocusNames=Tery_3866;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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: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; CP000393; ABG52905.1; -; Genomic_DNA.
DR   RefSeq; WP_011613235.1; NC_008312.1.
DR   AlphaFoldDB; Q10XW9; -.
DR   SMR; Q10XW9; -.
DR   STRING; 203124.Tery_3866; -.
DR   EnsemblBacteria; ABG52905; ABG52905; Tery_3866.
DR   KEGG; ter:Tery_3866; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_3; -.
DR   OMA; SYYQFQV; -.
DR   OrthoDB; 676868at2; -.
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..294
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000047525"
SQ   SEQUENCE   294 AA;  34080 MW;  51DA21DF55E21BDE CRC64;
     MNFQSVIATL NQFWSDRGCL IAQSYDTEKG AGTMNPHTFL RAIGPEPWSV AYVEPCRRPT
     DGRYGENPNR FQHYYQYQVL MKPSPNNIQD LYLDSLRALG IRPEDHDIRF VEDNWESPTL
     GAWGVGWEVW LDGMEITQFT YFQQCGSIDC RPVSIEITYG LERLAMYLQE VDAITKIAWT
     DNITYGDVYL QGEIEQCSYN FEASSPDFLF NLFGLYEQEA KQLIKRELVL PSLDYVLKCS
     HSFNLLDARG VISVTERTRY IGRIRNLARQ VGQLYLQQRE KLNFPLLKET MEAA