ID SYG_MYCPA Reviewed; 463 AA. AC Q73Y21; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 03-AUG-2022, 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}; Synonyms=glyS; GN OrderedLocusNames=MAP_2137c; OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) OS (Mycobacterium paratuberculosis). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium avium complex (MAC). OX NCBI_TaxID=262316; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-968 / K-10; RX PubMed=16116077; DOI=10.1073/pnas.0505662102; RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., RA Kanjilal S., Kapur V.; RT "The complete genome sequence of Mycobacterium avium subspecies RT paratuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005). 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}. 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; AE016958; AAS04454.1; -; Genomic_DNA. DR RefSeq; WP_010949492.1; NC_002944.2. DR AlphaFoldDB; Q73Y21; -. DR SMR; Q73Y21; -. DR STRING; 262316.MAP_2137c; -. DR EnsemblBacteria; AAS04454; AAS04454; MAP_2137c. DR KEGG; mpa:MAP_2137c; -. DR eggNOG; COG0423; Bacteria. DR HOGENOM; CLU_015515_2_1_11; -. DR OMA; EPSYGID; -. DR Proteomes; UP000000580; 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; Reference proteome. FT CHAIN 1..463 FT /note="Glycine--tRNA ligase" FT /id="PRO_0000072966" FT REGION 113..134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 102 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 165 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 197..199 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 207..212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 212..216 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 284..285 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 324..328 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" FT BINDING 328..331 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253" SQ SEQUENCE 463 AA; 52971 MW; F602B4C500CFEB2D CRC64; MHRLVASVID TVVNLAKRRG FVYPSGEIYG GTRSAWDYGP LGVEFKENIK RQWWRSVVTG REDVVGLDSS IILPRQVWVA SGHVEVFHDP LVESLITHKR YRADHLIEAY EAKHGHPPPN GLADIRDPDT GEPGRWTEPR EFNMMLKTYL GPIETEEGLH YLRPETAQGI FVNFANVVTT ARKKPPFGIG QIGKSFRNEI TPGNFIFRTR EFEQMEMEFF VEPSTAKEWH QYWIDTRLQW YVELGIDPQN LRLFEHPADK LSHYSDRTVD IEYKFGFAGN PWGELEGVAN RTDFDLSTHS KHSGVDLSFY DQATDSRYIP YVIEPAAGLT RSFMAFLIDA YVEDEAPNAK GKMEKRAVLR LDPRLAPVKA AVLPLSRHAD LSPKARDLAA ELRRFWNIEF DDAGAIGRRY RRQDEIGTPF CVTVDFDSLE DNAVTVRRRD DMSQERIGMD AVADYLSARL KGC //