ID   SYGA_AQUAE              Reviewed;         285 AA.
AC   O67081;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=aq_945;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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}.
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DR   EMBL; AE000657; AAC07050.1; -; Genomic_DNA.
DR   PIR; F70381; F70381.
DR   RefSeq; NP_213644.1; NC_000918.1.
DR   RefSeq; WP_010880582.1; NC_000918.1.
DR   PDB; 5F5W; X-ray; 2.81 A; A/B/C/D/E=1-285.
DR   PDBsum; 5F5W; -.
DR   AlphaFoldDB; O67081; -.
DR   SMR; O67081; -.
DR   STRING; 224324.aq_945; -.
DR   EnsemblBacteria; AAC07050; AAC07050; aq_945.
DR   KEGG; aae:aq_945; -.
DR   PATRIC; fig|224324.8.peg.742; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_0; -.
DR   InParanoid; O67081; -.
DR   OMA; SYYQFQV; -.
DR   OrthoDB; 676868at2; -.
DR   Proteomes; UP000000798; 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   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..285
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000072825"
FT   HELIX           3..16
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           32..34
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           36..39
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   STRAND          42..46
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   STRAND          48..57
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   STRAND          72..83
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           88..98
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   STRAND          108..117
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   STRAND          122..131
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   STRAND          134..145
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   STRAND          155..160
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           161..168
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           174..176
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   STRAND          178..180
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           185..201
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           206..226
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           229..248
FT                   /evidence="ECO:0007829|PDB:5F5W"
FT   HELIX           254..280
FT                   /evidence="ECO:0007829|PDB:5F5W"
SQ   SEQUENCE   285 AA;  33672 MW;  3D5F1F3F10282201 CRC64;
     MYFQDIIMTL HKFWAEKGCL IWQPYDVEVG AGTMNPATFL KVLGKKPWNV AYVEPSRRPQ
     DGRYGENPNR LQHYYQFQVI LKPAPRNPQE IYLESLERLG INPLEHDIRF VEDDWESPTL
     GAWGLGWEVW LDGMEITQFT YFQQAGGLDL DEISVEITYG LERIAMYIQD KDSVFDIEWK
     EGITYGEIFK RSEWEWSKYN FELADTDMLF QVYEMFEKES KRMVEEGLIF PAYDYLLKCS
     HVFNILDARG AISVQERARY IRRMNNLARE IAKLYLQVFE NVGAT