SYG_PYRAB
ID SYG_PYRAB Reviewed; 571 AA.
AC Q9V176; G8ZJ14;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=PYRAB05520;
GN ORFNames=PAB0380;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49474.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69941.1; -; Genomic_DNA.
DR PIR; C75174; C75174.
DR RefSeq; WP_010867676.1; NC_000868.1.
DR AlphaFoldDB; Q9V176; -.
DR SMR; Q9V176; -.
DR STRING; 272844.PAB0380; -.
DR PRIDE; Q9V176; -.
DR EnsemblBacteria; CAB49474; CAB49474; PAB0380.
DR GeneID; 1495454; -.
DR KEGG; pab:PAB0380; -.
DR PATRIC; fig|272844.11.peg.587; -.
DR eggNOG; arCOG00405; Archaea.
DR HOGENOM; CLU_015515_2_1_2; -.
DR OMA; EPSYGID; -.
DR OrthoDB; 32623at2157; -.
DR PhylomeDB; Q9V176; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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..571
FT /note="Glycine--tRNA ligase"
FT /id="PRO_0000072994"
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 571 AA; 66616 MW; 3CC82F80B8DA5E41 CRC64;
MGERFDKYEY LQDLMRRRGF AWGSFEIYGG SRGFYDYGPL GATIKRKIEK KIREAFIREG
FFEIETPDIT PEQVFIASGH VEKFVDPIVE CKKCGARFRA DHLIEETLGI DVEGKSAEEM
TKIIREHNIK CPECGGELGD VFYFNLMFET YIGPYKDKKA YLRPETAQGI FVNFKRLNAF
ARNKLPFGVF QIGKAYRNEI SPRQGMIRLR EFTQAEVEIF FNPNETEHPH FDEVKHEKLR
LYPIENQLKD LGMIELTAEE AVKKGYLMNT FFAYYLVMIK KILLDIGIPE DKIRFRQQLP
EERAHYSADT WDAEVYSERF GWVECVGLAY RTDYDLSRHM KMSGADLTVM IHYDKPKIVK
RLKVSLNMKS VGPKLKKDAK RINEKIQAMS EEELRELVKK LNEEGKIVID GYELSKDDFI
IKEVEEKVTG EKIIPHVLEP SFGIDRPFYL LLENSLTIDE DGRIYLKIKK DMAPIEVAVL
PLVAKEPLTK IAYDLFRKLQ KEGFIVVYDE KDSIGKRYMR YDEIGTPYCV TIDNQTPIDG
TVTIRDRDTR EQIRVKLEDV PRKLKELIFG S
