SYGA_ALKCK
ID SYGA_ALKCK Reviewed; 295 AA.
AC Q5WHD6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=ABC1684;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) 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; 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; AP006627; BAD64219.1; -; Genomic_DNA.
DR RefSeq; WP_011246528.1; NC_006582.1.
DR AlphaFoldDB; Q5WHD6; -.
DR SMR; Q5WHD6; -.
DR STRING; 66692.ABC1684; -.
DR EnsemblBacteria; BAD64219; BAD64219; ABC1684.
DR KEGG; bcl:ABC1684; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_9; -.
DR OMA; SYYQFQV; -.
DR OrthoDB; 676868at2; -.
DR Proteomes; UP000001168; 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; Reference proteome.
FT CHAIN 1..295
FT /note="Glycine--tRNA ligase alpha subunit"
FT /id="PRO_1000047399"
SQ SEQUENCE 295 AA; 34156 MW; C56F12984B778953 CRC64;
MNVQTMILTL QSFWAKQNCI ILNAYDTEKG AGTMSPHTLL RTIGPEPWNV AYVEPSRRPA
DGRYGENPNR LYQHHQFQVI MKPSPLNIQE LYLDSLRALG IDPLKHDIRF VEDNWENPTL
GCAGLGWEVW LDGMEITQFT YFQQVGGMEA NPVSAEITYG LERLATYIQD KENVFDLEWV
EGFTYGDIFL QPEYEHSTYT FEVSNVDMLF DLFSTYEKEA ERALARDLVF PAYDYILKCS
HSFNLLDARG AISVTERTGY IARVRTLARK AARKYYEERE KLGFPMLKKE DAHDE
