The YjeF C-terminal domain is an ~280-residue module found in the following proteins:

• Yeast chromosome XI hypothetical protein YKL151c.
• Caenorhabditis elegans hypothetical protein R107.2.
• Escherichia coli hypothetical protein YjeF.
• Bacillus subtilis hypothetical protein yxkO.
• Helicobacter pylori hypothetical protein HP1363.
• Mycobacterium tuberculosis hypothetical protein MtCY77.05c.
• Mycobacterium leprae hypothetical protein B229_C2_201.
• Synechocystis strain PCC 6803 hypothetical protein sll1433.
• Methanococcus jannaschii hypothetical protein MJ1586.
• Streptococcus mutans putative uncharacterized protein SMU.573.
• Streptococcus thermophilus predicted sugar kinase STER_0661.
• Streptococcus sanguinis putative uncharacterized protein SSA_0673.
• Thermotoga maritima hypothetical protein Tm0922.

The YjeF C-terminal domain has an α/β fold and shows high structural homology to the members of a ribokinase-like superfamily. The members of the ribokinase-like superfamily are all phosphotransferases and catalyze the phosphorylation of the hydroxymethyl group of the substrate; magnesium and ATP (or ADP) are required for their activity. The YjeF C-terminal is found in association with the YjeF N-terminal domain, which belongs of a specialized family of Rossmann fold domains (see <PDOC51385>) [1,2,3].

The first pattern we developed covers residues that might be involved in forming the substrate-binding pocket. The second one corresponds to residues that could form a kinase anion hole, with the conserved aspartate predicted to be the catalytic base [1]. We also developed a profile which covers the entire YjeF C-terminal domain.