SYGA_ACISJ
ID SYGA_ACISJ Reviewed; 317 AA.
AC A1W3F2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=Ajs_0527;
OS Acidovorax sp. (strain JS42).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX NCBI_TaxID=232721;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS42;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL Submitted (DEC-2006) 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; CP000539; ABM40777.1; -; Genomic_DNA.
DR RefSeq; WP_011803986.1; NC_008782.1.
DR AlphaFoldDB; A1W3F2; -.
DR SMR; A1W3F2; -.
DR STRING; 232721.Ajs_0527; -.
DR EnsemblBacteria; ABM40777; ABM40777; Ajs_0527.
DR KEGG; ajs:Ajs_0527; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_4; -.
DR OMA; SYYQFQV; -.
DR Proteomes; UP000000645; 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..317
FT /note="Glycine--tRNA ligase alpha subunit"
FT /id="PRO_1000047391"
SQ SEQUENCE 317 AA; 35632 MW; CDA3608A2706A065 CRC64;
MLTFQQIILK LQSYWADQGC ALLQPYDMEV GAGTSHTATF LRALGPEPWK AAYVQPSRRP
KDGRYGENPN RLQHYYQYQV VLKPAPDNIL ELYLGSLEAL GFDLKKNDIR FVEDDWENPT
LGAWGLGWEV WLNGMEVTQF TYFQQVGGID CKPATGEITY GLERLAMYLQ GVDNVYNLTW
TEGPNGAKLT YGDVYHQNEV EQSTYNFEHS DAEFLFTAFG AHEKQANHLM GEQLALPAYE
QVLKAAHTFN LLDARGAISV TERAAYIGRI RNLARAVAKA YLDSRARLGF PMAPKAHADE
VLAELAKAAE QQNKKAA