SYGA_DELAS
ID SYGA_DELAS Reviewed; 312 AA.
AC A9BXZ7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=Daci_1288;
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) 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; CP000884; ABX33932.1; -; Genomic_DNA.
DR RefSeq; WP_012203218.1; NC_010002.1.
DR AlphaFoldDB; A9BXZ7; -.
DR SMR; A9BXZ7; -.
DR STRING; 398578.Daci_1288; -.
DR PRIDE; A9BXZ7; -.
DR EnsemblBacteria; ABX33932; ABX33932; Daci_1288.
DR GeneID; 60685848; -.
DR KEGG; dac:Daci_1288; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_4; -.
DR OMA; SYYQFQV; -.
DR Proteomes; UP000000784; 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..312
FT /note="Glycine--tRNA ligase alpha subunit"
FT /id="PRO_1000101182"
SQ SEQUENCE 312 AA; 35062 MW; FA73BCCC79F9E615 CRC64;
MLTFQQIILK LQSYWADQGC ALLQPYDMEV GAGTSHTATF LRALGPEPWK AAYVQPSRRP
KDGRYGDNPN RLQHYYQFQV VLKPAPDNIL ELYLGSLEAL GFDLKKNDIR FVEDDWENPT
LGAWGLGWEV WLNGMEVTQF TYFQQVGGID CKPATGEITY GLERLAMYLQ GVDNVYNLTW
TDGLSYGDVY HQNEVEQSTY NFEHSDADFL FTAFGAYEKQ ANHLIGEQLA LPAYEQVLKA
AHTFNLLDAR GAISVTERAA YIGRIRNLAR AVAKAYMDSR ARLGFPMAPK AHADEVLAEL
AKAAEQQGKK AA