ID   SYG_METM7               Reviewed;         574 AA.
AC   A6VIK1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=MmarC7_1214;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-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.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00253}.
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DR   EMBL; CP000745; ABR66277.1; -; Genomic_DNA.
DR   RefSeq; WP_011977587.1; NC_009637.1.
DR   AlphaFoldDB; A6VIK1; -.
DR   SMR; A6VIK1; -.
DR   STRING; 426368.MmarC7_1214; -.
DR   EnsemblBacteria; ABR66277; ABR66277; MmarC7_1214.
DR   GeneID; 5327894; -.
DR   KEGG; mmz:MmarC7_1214; -.
DR   eggNOG; arCOG00405; Archaea.
DR   HOGENOM; CLU_015515_1_2_2; -.
DR   OMA; EPSYGID; -.
DR   OrthoDB; 32623at2157; -.
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..574
FT                   /note="Glycine--tRNA ligase"
FT                   /id="PRO_1000047378"
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   574 AA;  66015 MW;  B34E8C560845D6BC CRC64;
     MDKYDKIIDL TKRRGFLWNS FEIYGGIAGF FDYGPLGAIL KNNVINTWRK HYIVNEGFYE
     IDSPTVTPYE VLKASGHVEN FTDPLVECKE CLESFRADHI IEENVDVDTE GKTLQELQEM
     IEKNNIKCPK CGGEFKEVST FNLMFATSIG PGGKRAAFMR PETAQGIFIQ FKRISQFFRN
     KLPFGAVQIG KAYRNEISPR QGVIRLREFT QAEGEFFIDS RKKENFEKFE SVKDMVLPLL
     PGKNQENESL SAEEKIVRMS LSDAVKNGVI AHEAIAYYVA VTKKFLMEIG IDESKLRFRQ
     HLPNEMAHYA ADCWDAELYT DRYGWIECVG IADRTNYDLL AHMKNSSEDL SVFVELDEDK
     EVEVYEIELN YKLVGRTFKG DAKILEESLK ELNDKKMEEL VEALETEGKY VLKTCKRDFE
     ILKEYLTAKK VKKIVKGEKI IPHVIEPSYG IDRITYCVME HAFKEEEDRT VMGFSNAVSP
     IKVGVFPLVN KEGMPEIAMD LKNKLRENGL IAEYDDSGAI GRRYMRMDEV GTPFCVTIDG
     ETLTDRSVTI RERDSREQFR IPINEVVSYI KDKL