SYG_THEKO
ID SYG_THEKO Reviewed; 570 AA.
AC Q5JID8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=TK0978;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00253}.
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DR EMBL; AP006878; BAD85167.1; -; Genomic_DNA.
DR RefSeq; WP_011249929.1; NC_006624.1.
DR AlphaFoldDB; Q5JID8; -.
DR SMR; Q5JID8; -.
DR IntAct; Q5JID8; 1.
DR MINT; Q5JID8; -.
DR STRING; 69014.TK0978; -.
DR EnsemblBacteria; BAD85167; BAD85167; TK0978.
DR GeneID; 3235345; -.
DR KEGG; tko:TK0978; -.
DR PATRIC; fig|69014.16.peg.956; -.
DR eggNOG; arCOG00405; Archaea.
DR HOGENOM; CLU_015515_1_0_2; -.
DR InParanoid; Q5JID8; -.
DR OMA; EPSYGID; -.
DR OrthoDB; 32623at2157; -.
DR PhylomeDB; Q5JID8; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd00774; GlyRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
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; Reference proteome.
FT CHAIN 1..570
FT /note="Glycine--tRNA ligase"
FT /id="PRO_0000072997"
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; 66680 MW; 9470E585FDFE03F4 CRC64;
MGEKPDKYEI LQDLMRRRGF AWGSFEIYGG SRGFYDYGPL GATIKRKIER KIREAFQREG
FFELETPDIT PEKVFIASGH VEKFVDPLVE CKKCGARFRA DHLVEEALGI DTEGMSAEHL
TQLIREHDIR CPECGGELSD VWYFNLMFET RIGPYGDQKG YLRPETAQGI FVNFRRLNAF
ARNKLPFGVF QIGKAYRNEI SPRQGMLRLR EFTQAEAEIF FNPNETEHPH FDEVKDEKLR
LYPIEHQLKN LSMIELTAEE AVKKGYIMNT FFAYYMVMVK RVLLDIGIPE DKIRFRQQLP
EERAHYSRDT WDAEIHSERF GWVECVGIAN RGDYDLSRHM RESGADLTVL IHYDEPKIVK
KLEVSLNMKR VGPKLKKDAK RINELIKGWG EEKKRELVEL LEKEGKVTIE GYELEKDDFI
IREVEEKITG EKIVPHVLEP SFGIDRPFYL LLENSLVIEE DRTYLRIKKD MAPIEVAVLP
LVAKEPLKSI AYDIFRTLQK EGFIAVYDEK DTVGRRYMRY DEIGTPYCVT VDNQTPEDGT
VTIRDRDTRE QIRVKIEELP KKLRELIFES
