SYG_METM5
ID SYG_METM5 Reviewed; 575 AA.
AC A4FZX1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=MmarC5_1458;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000609; ABO35755.1; -; Genomic_DNA.
DR RefSeq; WP_011869205.1; NC_009135.1.
DR AlphaFoldDB; A4FZX1; -.
DR SMR; A4FZX1; -.
DR STRING; 402880.MmarC5_1458; -.
DR PRIDE; A4FZX1; -.
DR EnsemblBacteria; ABO35755; ABO35755; MmarC5_1458.
DR GeneID; 4927579; -.
DR KEGG; mmq:MmarC5_1458; -.
DR eggNOG; arCOG00405; Archaea.
DR HOGENOM; CLU_015515_1_2_2; -.
DR OMA; EPSYGID; -.
DR OrthoDB; 32623at2157; -.
DR Proteomes; UP000000253; 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; -; 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.
FT CHAIN 1..575
FT /note="Glycine--tRNA ligase"
FT /id="PRO_1000047377"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 194..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 204..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 209..213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 327..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 446..450
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 450..453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
SQ SEQUENCE 575 AA; 65991 MW; 1F30E1158AEC336F CRC64;
MDKYDKIIDL TKRRGFLWNS FEIYGGIAGF FDYGPLGAIL KNNVINTWRK HYIVNEGFYE
IDSPTVTPYE VLKASGHVEN FTDPLVECKS CLESFRADHI IEENVDVDTE GKTLQELQEM
IEKNNIKCPK CGGEFKEVST FNLMFATSIG PGGKRAAFMR PETAQGIFIQ FKRISQFFRN
KLPFGAVQIG KAYRNEISPR QGVIRLREFT QAEGEFFIDS RKKENFEKFE SVKEIVLPLL
SGKNQENESL SAEEKIVRMS LSDAVKNGII AHEAIAYYIA VTKKFLMEIG IDESKLRFRQ
HLPNEMAHYA ADCWDAELYT DRYGWIECVG IADRTNYDLL AHMKNSSEDL SVFVELDEDK
EIEVYEIELN YKLVGRTFKG DSKVLEESLK ELDDKKMEEL VEALETEGKY VLSTCKRDFE
LLKEYLTAKK VKKTVKGEKI IPHVIEPSYG IDRITYCVME HAFKEDEDRT VMGFSNAVSP
IKVGVFPLVN KEGMPEIAMD LKNKLRENGL IAEYDDSGAI GRRYMRMDEV GTPFCVTIDG
ETLTDSSVTI RERDSREQFR IPINEVVPYI KDKLN
