RNA helicase, ATP-dependent, DEAD-box, conserved site <p>A number of eukaryotic and prokaryotic proteins involved in ATP-dependent, nucleic-acid unwinding have been characterised [<cite idref="PUB00003826"/>, <cite idref="PUB00004037"/>, <cite idref="PUB00004089"/>] on the basis of their structural similarity. All these proteins share a number of conserved sequence motifs. Some of them are specific to this family while others are shared by other ATP-binding proteins or by proteins belonging to the helicases `superfamily'[<cite idref="PUB00004025"/>]. One of these motifs, called the 'D-E-A-D-box', represents a special version of the B motif of ATP-binding proteins. Proteins currently known to belong to this family include eukaryotic initiation factor eIF-4A; yeast PRP5, PRP28 and MSS116 splicing proteins, and proteins DHH1, DRS1, MAK5 and ROK1; mouse Pl10, <taxon tax_id="6239">Caenorhabditis elegans</taxon> helicase glh-1; Drosophila Rm62 (p62), Me31B and Vasa; and <taxon tax_id="562">Escherichia coli</taxon> putative RNA helicases dbpA, deaD, rhlB and rhlE.</p>