ID   SYGA_DICT6              Reviewed;         299 AA.
AC   B5YES5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=DICTH_1204;
OS   Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12).
OC   Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=309799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35947 / DSM 3960 / H-6-12;
RX   PubMed=24558247; DOI=10.1128/genomea.00109-14;
RA   Coil D.A., Badger J.H., Forberger H.C., Riggs F., Madupu R., Fedorova N.,
RA   Ward N., Robb F.T., Eisen J.A.;
RT   "Complete Genome Sequence of the Extreme Thermophile Dictyoglomus
RT   thermophilum H-6-12.";
RL   Genome Announc. 2:0-0(2014).
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; CP001146; ACI18824.1; -; Genomic_DNA.
DR   RefSeq; WP_012547456.1; NC_011297.1.
DR   AlphaFoldDB; B5YES5; -.
DR   SMR; B5YES5; -.
DR   STRING; 309799.DICTH_1204; -.
DR   EnsemblBacteria; ACI18824; ACI18824; DICTH_1204.
DR   KEGG; dth:DICTH_1204; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_0; -.
DR   OMA; SYYQFQV; -.
DR   OrthoDB; 676868at2; -.
DR   Proteomes; UP000001733; 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.
FT   CHAIN           1..299
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000101185"
SQ   SEQUENCE   299 AA;  34964 MW;  AF124FB3703A665D CRC64;
     MLFQEIIFKL NEFWHKQGCI IQQPYDIEVG AGTMNPATFF RVLGPEPWYV AYVEPSRRPT
     DGRYGENPNR LQHYYQYQVI LKPSPANVQE IYIESLEYLG IDIEKHDIRF VEDNWESPTL
     GAWGIGWEVW LDGMEITQFT YFQQCGGFDL FPISAEITYG LERIAMYIQG IDDFKDIKWQ
     DGITYGDIHL QSEVENCIYN FELADVERLR LLFNEYEKEA ERLLNEGLTF PGYDYVLKCS
     HTFNLLDARG AISVVQRSQY ISRIRRLAAK AAENYLKSRE ALGFPLLNKA WRKEEAQIG