|PROSITE documentation PDOC51385 [for PROSITE entry PS51385]|
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:
The profile we developed covers the entire YjeF N-terminal domain.Last update:
June 2008 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Anantharaman V. Aravind L.|
|Title||Novel conserved domains in proteins with predicted roles in eukaryotic cell-cycle regulation, decapping and RNA stability.|
|Source||BMC Genomics 5:45-45(2004).|
|2||Authors||Jha K.N. Shumilin I.A. Digilio L.C. Chertihin O. Zheng H. Schmitz G. Visconti P.E. Flickinger C.J. Minor W. Herr J.C.|
|Title||Biochemical and structural characterization of apolipoprotein A-I binding protein, a novel phosphoprotein with a potential role in sperm capacitation.|