ID   SYG_UREU1               Reviewed;         473 AA.
AC   B5ZC00;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=glyQS {ECO:0000255|HAMAP-Rule:MF_00253}; OrderedLocusNames=UUR10_0564;
OS   Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=565575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33699 / Western;
RA   Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT   "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL   Submitted (OCT-2008) 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   -!- SUBUNIT: Homodimer. {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; CP001184; ACI60310.1; -; Genomic_DNA.
DR   RefSeq; WP_004025511.1; NC_011374.1.
DR   AlphaFoldDB; B5ZC00; -.
DR   SMR; B5ZC00; -.
DR   STRING; 565575.UUR10_0564; -.
DR   EnsemblBacteria; ACI60310; ACI60310; UUR10_0564.
DR   GeneID; 45016094; -.
DR   KEGG; uue:UUR10_0564; -.
DR   eggNOG; COG0423; Bacteria.
DR   HOGENOM; CLU_015515_2_0_14; -.
DR   OMA; EPSYGID; -.
DR   OrthoDB; 626850at2; -.
DR   Proteomes; UP000002018; 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_B; Gly_tRNA_synth_B; 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; IPR022961; Gly_tRNA_ligase_bac.
DR   InterPro; IPR033731; GlyRS-like_core.
DR   InterPro; IPR002315; tRNA-synt_gly.
DR   PANTHER; PTHR10745; PTHR10745; 3.
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..473
FT                   /note="Glycine--tRNA ligase"
FT                   /id="PRO_1000101170"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         204..206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         214..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         219..223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         289..290
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         329..333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         333..336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
SQ   SEQUENCE   473 AA;  55372 MW;  B7E83B22CD516A5D CRC64;
     MKNKFKTQEE LVNHLKTVGF VFANSEIYNG LANAWDYGPL GVLLKNNLKN LWWKEFVTKQ
     KDVVGLDSAI ILNPLVWKAS GHLDNFSDPL IDCKNCKARY RADKLIESFD ENIHIAENSS
     NEEFAKVLND YEISCPTCKQ FNWTEIRHFN LMFKTYQGVI EDAKNVVYLR PETAQGIFVN
     FKNVQRSMRL HLPFGIAQIG KSFRNEITPG NFIFRTREFE QMEIEFFLKE ESAYDIFDKY
     LNQIENWLVS ACGLSLNNLR KHEHPKEELS HYSKKTIDFE YNFLHGFSEL YGIAYRTNYD
     LSVHMNLSKK DLTYFDEQTK EKYVPHVIEP SVGVERLLYA ILTEATFIEK LENDDERILM
     DLKYDLAPYK IAVMPLVNKL KDKAEEIYGK ILDLNISATF DNSGSIGKRY RRQDAIGTIY
     CLTIDFDSLD DQQDPSFTIR ERNSMAQKRI KLSELPLYLN QKAHEDFQRQ CQK