|Function||glutamyl-tRNA(Gln) amidotransferase, subunit E|
|Domain Trusted Cutoff||319.55|
|Domain Noise Cutoff||223.40|
|Mainrole Category||Protein synthesis|
|Subrole Category||tRNA aminoacylation|
|Gene Ontology Term||GO:0006424: glutamyl-tRNA aminoacylation biological_process|
| ||GO:0050567: glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity molecular_function|
|Entry Date||Apr 20 1999 2:07PM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||This peptide is found only in the Archaea. It is paralogous to the gatB-encoded subunit of Glu-tRNA(Gln) amidotransferase. The GatABC system operates in many bacteria to convert Glu-tRNA(Gln) into Gln-tRNA(Gln). However, the homologous system in archaea instead converts Asp-tRNA(Asn) to Asn-tRNA(Asn). Glu-tRNA(Gln) is converted to Gln-tRNA(Gln) by a heterodimeric amidotransferase of GatE (this protein) and GatD.
The Archaea have an Asp-tRNA(Asn) amidotransferase instead of an Asp--tRNA ligase, but the genes have not been identified. It is likely that this protein replaces gatB in Asp-tRNA(Asn) amidotransferase but that both enzymes share gatA.|
|References||DR PROSITE; PDOC00948;
DR PFAM; PF01162; PET112 family, C terminal region
RT Domain-specific recruitment of amide amino acids for protein synthesis.
RA Tumbula DL, Becker HD, Chang WZ, Soll D.
RL Nature. 2000 Sep 7;407(6800):106-10.
DR HAMAP; MF_00588; 29 of 29|
|Genome Property||GenProp0258: tRNA aminoacylation (HMM)|
| ||GenProp0831: archaeal core gene set, exactly 1 per genome (HMM)|
© J. Craig Venter Institute | Privacy Statement | Data Disclaimer