PROSITE documentation PDOC51385

YjeF N-terminal domain profile

The YjeF N-terminal domains occur either as single proteins or fusions with other domains and are commonly associated with enzymes. In bacteria and archaea, YjeF N-terminal domains are often fused to a YjeF C-terminal domain with high structural homology to the members of a ribokinase-like superfamily (see <PDOC00806>) and/or belong to operons that encode enzymes of diverse functions: pyridoxal phosphate biosynthetic protein PdxJ; phosphopanteine-protein transferase; ATP/GTP hydrolase; and pyruvate-formate lyase 1-activating enzyme. In plants, the YjeF N-terminal domain is fused to a C-terminal putative pyridoxamine 5'-phosphate oxidase. In eukaryotes, proteins that consist of (Sm)-FDF-YjeF N-terminal domains may be involved in RNA processing [1,2].

The YjeF N-terminal domains represent a novel version of the Rossmann fold, one of the most common protein folds in nature observed in numerous enzyme families, that has acquired a set of catalytic residues and structural features that distinguish them from the conventional dehydrogenases. The YjeF N-terminal domain is comprised of a three-layer α-β-α sandwich with a central β-sheet surrounded by helices (see <PDB:2O8N>). The conservation of the acidic residues in the predicted active site of the YjeF N-terminal domains is reminiscent of the presence of such residues in the active sites of diverse hydrolases [1,2].

Some proteins known to contain a YjeF N-terminal domain are listed below:

• Escherichia coli hypothetical protein YjeF.
• Thermotoga maritima hypothetical protein Tm0922.
• Yeast uncharacterized protein YNL200C.
• Yeast enhancer of mRNA-decapping protein 3 (EDC3).
• Vertebrate enhancer of mRNA-decapping protein 3 (EDC3).
• Mammalian apolipoprotein A-I binding protein (AI-BP), a protein that interacts with apolipoprotein A-I, a major constituent of high-density lipoprotein (HDL).

The profile we developed covers the entire YjeF N-terminal domain.