EF1 guanine nucleotide exchange domain
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| EF1_GNE | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 yeast guanine nucleotide exchange factor eef1balpha k205a mutant in complex with eef1a | |||||||||
| Identifiers | |||||||||
| Symbol | EF1_GNE | ||||||||
| Pfam | PF00736 | ||||||||
| InterPro | IPR014038 | ||||||||
| PROSITE | PDOC00648 | ||||||||
| SCOP2 | 1b64 / SCOPe / SUPFAM | ||||||||
| CDD | cd00292 | ||||||||
| |||||||||
In molecular biology, the EF1 guanine nucleotide exchange domain is a protein domain found in the beta and delta chains of elongation factors from eukaryotes and archaea.
Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta).[1]
The EF1 guanine nucleotide exchange domain is found in the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).[2]