Description

IPR004161 is a Translation elongation factor EFTu-like, domain 2.

<p>This entry represents a domain found in a number of translation factors that is homologous to domain 2 of EF2-Tu (also known as EF1A and EF-1alpha).</p> <p>EF2-Tu (EF1A) consists of three structural domains. This entry represents domain 2, which adopts a β-barrel structure, and is involved in binding to both charged tRNA [[cite:PUB00007398]]. This domain is structurally related to the C-terminal domain of EF2-Tu ([interpro:IPR004160]), to which it displays weak sequence matches. This domain is also found in other proteins such as translation initiation factor IF-2 and tetracycline-resistance proteins.</p> <p>EF-Tu (also known as EF-1alpha or EF1A) is a G-protein. It forms a ternary complex of EF-Tu (EF1A)-GTP-aminoacyltRNA. The binding of aminoacyl-tRNA stimulates GTP hydrolysis by EF-Tu (EF1A), causing a conformational change in EF-Tu (EF1A) that causes EF-Tu (EF1A)-GDP to detach from the ribosome, leaving the aminoacyl-tRNA attached at the A-site. Only the cognate aminoacyl-tRNA can induce the required conformational change in EF-Tu (EF1A) through its tight anticodon-codon binding [[cite:PUB00033960], [cite:PUB00033961]]. EF-Tu (EF1A)-GDP is returned to its active state, EF-Tu (EF1A)-GTP, through the action of another elongation factor, EF1B (also known as EF-Ts or EF-1beta/gamma/delta).</p> <p>Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [[cite:PUB00033953], [cite:PUB00033952], [cite:PUB00033951]]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 100