ID   SYGA_DESPS              Reviewed;         290 AA.
AC   Q6AS28;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   18-JUN-2025, entry version 100.
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=DP0118;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
OC   Desulfobulbales; Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG34847.1; -; Genomic_DNA.
DR   RefSeq; WP_011187363.1; NC_006138.1.
DR   AlphaFoldDB; Q6AS28; -.
DR   SMR; Q6AS28; -.
DR   STRING; 177439.DP0118; -.
DR   KEGG; dps:DP0118; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_7; -.
DR   OrthoDB; 9802183at2; -.
DR   Proteomes; UP000000602; Chromosome.
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; Reference proteome.
FT   CHAIN           1..290
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000047415"
SQ   SEQUENCE   290 AA;  33533 MW;  21856076BE83A74D CRC64;
     MNFQNIIFEL NNYWAEQGCV VQQPYDMEVG AGTFHPATLL RSLGPEPWKA AYAQPSRRPT
     DGRYGENPNR LQHYYQYQVV MKPSPLNIQE LYLGSLKRFG LNLLEHDIRF VEDDWESPTL
     GASGLGWEIW LDGMEISQFT YFQQAGSIDL TPTTVEITYG LERIAMYLQG VESVYDIAWN
     DEVTYGEIFH QAEVEFSTFN FEEANVEKLT DFFNSFEEEA HKLIAKKLIL PAYDYCLKCS
     HTFNLLDARK AISVTERTRY IGRIRNIARG VAEQYVIQRA ELGHPLIKNK
//