ID SYG_STAA3 Reviewed; 463 AA. AC Q2FGF8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 02-SEP-2026, entry version 108. 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}; GN OrderedLocusNames=SAUSA300_1525; OS Staphylococcus aureus (strain USA300). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USA300; RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(2006). CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). CC {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Gly) + glycine + ATP = glycyl-tRNA(Gly) + AMP + CC diphosphate; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000255; ABD22244.1; -; Genomic_DNA. DR RefSeq; WP_001030080.1; NZ_CP027476.1. DR AlphaFoldDB; Q2FGF8; -. DR SMR; Q2FGF8; -. DR KEGG; saa:SAUSA300_1525; -. DR HOGENOM; CLU_015515_2_1_9; -. DR OMA; MEMQYFV; -. DR Proteomes; UP000001939; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA. DR GO; GO:0070062; C:extracellular exosome; IEA:UniProtKB-ARBA. DR GO; GO:1990742; C:microvesicle; IEA:UniProtKB-ARBA. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IEA:UniProtKB-ARBA. DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProtKB-ARBA. DR GO; GO:0004820; F:glycine-tRNA ligase activity; ISS:UniProtKB. DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-ARBA. DR GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; IEA:UniProtKB-ARBA. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00774; GlyRS-like_core; 1. DR CDD; cd00858; GlyRS_anticodon; 1. DR FunFam; 3.40.50.800:FF:000002; Glycine--tRNA ligase; 1. DR Gene3D; 3.30.40.230; -; 1. DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 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; IPR060648; GlyRS_ins_1. DR InterPro; IPR002315; tRNA-synt_gly. DR NCBIfam; TIGR00389; glyS_dimeric; 1. DR NCBIfam; NF003211; PRK04173.1; 1. DR PANTHER; PTHR10745:SF8; DNA POLYMERASE SUBUNIT GAMMA-2, MITOCHONDRIAL; 1. DR PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 1. DR Pfam; PF28494; GlyRS_ins_1; 2. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01043; TRNASYNTHGLY. DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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..463 FT /note="Glycine--tRNA ligase" FT /id="PRO_1000047384" FT BINDING 98 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 174 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 206..208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 216..221 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 221..225 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 290..291 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 330..334 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 334..337 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" SQ SEQUENCE 463 AA; 53620 MW; F873C180BC51C467 CRC64; MAKDMDTIVS LAKHRGFVFP GSDIYGGLSN TWDYGPLGVE LKNNVKKAWW QKFITQSPFN VGIDAAILMN PKVWEASGHL NNFNDPMIDN KDSKIRYRAD KLIEDYMQDV KGDENFIADG LSFEQMKKII DDEGIVCPVS KTANWTEIRQ FNLMFKTFQG VTEDSTNEIF LRPETAQGIF VNYKNVQRSM RKKLPFGIGQ IGKSFRNEIT PGNFIFRTRE FEQMELEFFC KPGEEIEWQN YWKTFASDWL TSLNMSSENM RLRDHDEDEL SHYSNATTDI EYKFPFGWGE LWGIASRTDF DLRKHAEHSG EDFRYHDPET NEKYIPYCIE PSLGADRVTL AFLCDAYDEE GVEGSKDART VLHFHPALAP YKAAILPLSK KLSGEAIKIF EQLSSKFSID FDESQSIGKR YRRQDEIGTP YCVTFDFDSL EDNQVTVRDR DSMEQVRMPI SELEAFLTEK TKF //