ID   SYGA_MORCA              Reviewed;         318 AA.
AC   P77892;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   18-JUN-2025, entry version 99.
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;
OS   Moraxella catarrhalis (Branhamella catarrhalis).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Moraxellales; Moraxellaceae; Moraxella.
OX   NCBI_TaxID=480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25238 / DSM 9143 / BCRC 10629 / CCUG 353 / CIP 73.21 /
RC   NCTC 11020 / Ne 11;
RA   Walker E.S., Preston R.A., Post J.C., Ehrlich G.D., Klingman K.L.;
RL   Submitted (NOV-1996) 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;
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; U73324; AAB18211.1; -; Genomic_DNA.
DR   AlphaFoldDB; P77892; -.
DR   SMR; P77892; -.
DR   eggNOG; COG0752; Bacteria.
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..318
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000072849"
SQ   SEQUENCE   318 AA;  36235 MW;  B34405FD84F06768 CRC64;
     MDSGETLTFQ ALILTLQNYW ASRGCVVLQP YDMEVGAGTF HTATFLRALT PERWNTAYVQ
     PSRRPTDGRY GDNPNRLQHY YQFQVVLKPN PANIQELYLG SLKAIGIDTL THDVRFVEDN
     WESPTLGAWG LGWEVWLNGM EVTQFTYFQQ VGGIECFPVT GEITYGLERL AMYIQGVDSV
     YDLVWADGEF GRVTYGDVFH QNEVEQSAYN FEHADVAKLF ELFDFYEEQA DKLVAVNLPL
     PAYEMVLKAS HAFNLLDARG AISVTERQRF ILRVRTLARK VAISYTEARA KLGFPLADDA
     HKAEALEKWL PKEPKIIL
//