ID   SYG_PYRFU               Reviewed;         568 AA.
AC   Q8U0G2;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=PF1627;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81751.1; -; Genomic_DNA.
DR   RefSeq; WP_011012774.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U0G2; -.
DR   SMR; Q8U0G2; -.
DR   STRING; 186497.PF1627; -.
DR   EnsemblBacteria; AAL81751; AAL81751; PF1627.
DR   GeneID; 41713452; -.
DR   KEGG; pfu:PF1627; -.
DR   PATRIC; fig|186497.12.peg.1694; -.
DR   eggNOG; arCOG00405; Archaea.
DR   HOGENOM; CLU_015515_2_1_2; -.
DR   OMA; EPSYGID; -.
DR   OrthoDB; 32623at2157; -.
DR   PhylomeDB; Q8U0G2; -.
DR   Proteomes; UP000001013; 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; Reference proteome.
FT   CHAIN           1..568
FT                   /note="Glycine--tRNA ligase"
FT                   /id="PRO_0000072995"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         195..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         205..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         210..214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         322..323
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         437..441
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         441..444
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
SQ   SEQUENCE   568 AA;  66399 MW;  25B5962BAF16D3F9 CRC64;
     MKFDKYEYLQ DLMRRRGFAW GSFEIYGGAR GFYDYGPLGA TIKRKIEKKI REAFIREGFF
     EIETPDITPE QVFIASGHVE KFVDPLVECK KCGARFRADH LIEETLGIDV EGKSAEEMTK
     IIREHNIRCP ECGGELSDVW YFNLMFETYI GPYKDKKAYL RPETAQGIFV NFKRLNAFAR
     NKLPFGVFQI GKAYRNEISP RQGMIRLREF TQAEVEIFFN PNETEHPHFD EVKDEVLRLY
     PIEHQLKDLG MIELTAEEAV KKGYVMNTFF AYYMVMIKRI LLDIGIPEDK IRFRQQLPEE
     RAHYSADTWD AEIYSERFGW VECVGLAYRT DYDLSRHMKM SGADLTVMIH YDKPKIVKKL
     NVTLNMKKVG PKLKEKVKEI NEKLKSMSQE ELRKLVEELN ANGKVIIEGH ELEKEDLIIK
     EVEEKIQGEK IVPHVLEPSF GIDRPFYLLL ENSLTVDEDG RVYLKIKKDM APIEVAVLPL
     VAKEPLTTIA YEIYRNLQKE GFIVVYDEKD SIGKRYMRYD EIGTPYCVTV DNQTPEDGTV
     TIRDRDTREQ IRVKIEEVPR KLKELIFG