SYG_THEGJ
ID SYG_THEGJ Reviewed; 570 AA.
AC C5A1H0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Glycine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00253};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00253};
DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00253};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00253};
GN Name=glyS {ECO:0000255|HAMAP-Rule:MF_00253}; OrderedLocusNames=TGAM_1737;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly).
CC {ECO:0000255|HAMAP-Rule:MF_00253}.
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_00253};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00253}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00253}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001398; ACS34239.1; -; Genomic_DNA.
DR RefSeq; WP_015859349.1; NC_012804.1.
DR AlphaFoldDB; C5A1H0; -.
DR SMR; C5A1H0; -.
DR STRING; 593117.TGAM_1737; -.
DR PaxDb; C5A1H0; -.
DR PRIDE; C5A1H0; -.
DR EnsemblBacteria; ACS34239; ACS34239; TGAM_1737.
DR GeneID; 7987456; -.
DR KEGG; tga:TGAM_1737; -.
DR PATRIC; fig|593117.10.peg.1744; -.
DR eggNOG; arCOG00405; Archaea.
DR HOGENOM; CLU_015515_1_2_2; -.
DR OMA; EPSYGID; -.
DR OrthoDB; 32623at2157; -.
DR Proteomes; UP000001488; 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; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00774; GlyRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 2.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00253_A; Gly_tRNA_synth_A; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR022960; Gly_tRNA_ligase_arc.
DR InterPro; IPR033731; GlyRS-like_core.
DR InterPro; IPR002315; tRNA-synt_gly.
DR PANTHER; PTHR10745; PTHR10745; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..570
FT /note="Glycine--tRNA ligase"
FT /id="PRO_1000204582"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 197..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 207..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 212..216
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 324..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 439..443
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 443..446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
SQ SEQUENCE 570 AA; 66518 MW; 6E9CF6AE387EB779 CRC64;
MGEKPDKYEI LQDLMRRRGF AWGSFEIYGG SRGFYDYGPL GATIKRKIEQ KIREAFQREG
FFELETPDIT PEKVFIASGH VEKFVDPLVE CRKCGARFRA DHIIEEALGM DVEGLSAEEL
TKLIREHDIR CPECGGELSD VWYFNLMFET KIGPYGDQKG YLRPETAQGI FVNFKRLNAF
ARNKLPFGVF QIGKAYRNEI SPRQGMLRLR EFTQAEAEIF FNPSETEHPH FDEVKNEKLR
LYPIEHQLKN LGEIELTAEE AVKKGYIMNT FFAYYMVMVK RVLLDIGIPE DKIRFRQQLP
EERAHYSRDT WDAEVHSERF GWVECVGIAN RGDYDLSRHM RESGADLTVL IHYDEPKIVK
RLEVSLNLKR VGPKLRKDAK RINELIKSWN EEKKRELVEI LGKEGKITIE GYELEKDDFI
IREVEEKITG EKIVPHVLEP SFGIDRPFYL LLENSLVIEE DRTYLKLKKD MAPIEVAVLP
LVAKEPLKSI AYEIFRKLQK AGFIVVYDEK DTIGRRYLRY DEIGTPYCVT IDNQTPEDST
VTIRDRDTRE QVRVSIEELP SKLRELIFGE
