SYGA_MORCA
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 03-AUG-2022, entry version 87.
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; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=480;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25238 / DSM 9143 / BCRC 10629 / CIP 73.21 / 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=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; U73324; AAB18211.1; -; Genomic_DNA.
DR AlphaFoldDB; P77892; -.
DR SMR; P77892; -.
DR STRING; 857571.EA1_07735; -.
DR PRIDE; P77892; -.
DR eggNOG; COG0752; Bacteria.
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..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