SPM_001915
  | Uniprot: A0A037UT54
Description: glutamyl-tRNA amidotransferase EC number: Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. {ECO:0000256|SAAS:SAAS00573105}.; CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. {ECO:0000256|SAAS:SAAS00512389}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). {ECO:0000256|SAAS:SAAS00573109}. Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): Gene names (synonym): Mass: 11,197 Subunit structure [CC]: SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000256|SAAS:SAAS00573103}. Gene ontology (GO): ATP binding [GO:0005524]; ligase activity [GO:0016874]; transferase activity [GO:0016740]; regulation of translational fidelity [GO:0006450]; translation [GO:0006412] Gene ontology IDs: GO:0005524; GO:0006412; GO:0006450; GO:0016740; GO:0016874 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the GatC family. {ECO:0000256|SAAS:SAAS00573107}. Protein families: GatC family Coiled coil: Domain [FT]: Motif: Region: EMBL: AGBZ02000001 ProteinModelPortal: MEROPS: EnsemblBacteria KO: KAI92790 UniPathway: CDD: Gene3D: HAMAP: InterPro: PANTHER: IPR003837 PIRSF: PRINTS: PROSITE: Pfam: ProDom: PF02686 SMART: SUPFAM: TIGRFAMs: SSF141000 |
349435-349729(-) >nucleotide sequence AATTTCAGCTTGTGGAGCAACATCAATTTCATCATCCTCACGCAAATAGTCAACTGTTAA GTCAAATGGAAAATGCATTGAATGAACATTAGTTGTATTAATTTTTTGTACTAAATCCAT TTGCTTTAAAATAACATCAAATTCTTGACTTAAATTAGTTAGTTCCTCATCTTGTAAATC TAGCATAATATCATGTGCTAACATCTGTAGCACTTCTTTTGTAATTCGTGCCAT >protein sequence VDYLREDDEIDVAPQAEILAAAPKKIDDYIVINKVVK |
© Fisunov Lab of Proteomics, 2016.