AC MF_02076; DC Protein; auto TR HAMAP; MF_02076; -; 1; level=0 XX Names: Glu_tRNA_synth_type2 XX ID SYE DE RecName: Full=Glutamate--tRNA ligase; DE EC=6.1.1.17; DE AltName: Full=Glutamyl-tRNA synthetase; DE Short=GluRS; GN Name=gltX; XX CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two- CC step reaction: glutamate is first activated by ATP to form Glu-AMP and CC then transferred to the acceptor end of tRNA(Glu). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L- CC glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, CC Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, CC ChEBI:CHEBI:456215; EC=6.1.1.17; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC Glutamate--tRNA ligase type 2 subfamily. XX DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1; trigger=no DR Pfam; PF00749; tRNA-synt_1c; 1; trigger=no DR Pfam; PF03950; tRNA-synt_1c_C; 1; trigger=no DR PRINTS; PR00987; TRNASYNTHGLU; 1; trigger=no DR NCBIfam; TIGR00463; gltX_arch; 1; trigger=no XX KW Aminoacyl-tRNA synthetase KW ATP-binding KW Cytoplasm KW Ligase KW Nucleotide-binding KW Protein biosynthesis XX GO GO:0005524; F:ATP binding GO GO:0004818; F:glutamate-tRNA ligase activity GO GO:0006424; P:glutamyl-tRNA aminoacylation GO GO:0005737; C:cytoplasm XX FT From: SYE_METJA (Q58772) FT MOTIF 98..108 FT /note="'HIGH' region" FT Condition: P-[SNE]-P-x(4)-[HTS]-[LIVM]-G-x XX Size: 530-640; Related: MF_01428; Template: P04805; O25360; P27000; Q8DLI5; Scope: Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: This signature is specific for archaeal and eukaryotic cytoplasmic glutamate--tRNA ligases. See MF_00022 for bacterial and eukaryotic mitochondrial glutamate--tRNA ligases. XX # Revision 1.5 2023/06/01 //