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. 2006 Aug 25;34(15):4206–4215. doi: 10.1093/nar/gkl460

Figure 1.

Figure 1

A schematic alignment of the human homologues of the DExD/H box proteins considered in this review, highlighting the different lengths of the divergent N- and C-terminal domains. The conserved helicase cores [in yellow for DExH and light blue for DEAD (DEVD in the case of Ddx21)] are shown, with the conserved motifs within them numbered (I–VI) and highlighted in dark blue. The number of amino acids in the helicase cores and the N- and C-terminal domains are indicated for each protein. The functions of the conserved motifs are as follows: Motifs Q, I, II and VI are required for ATP binding and hydrolysis; motifs Ia, Ib, III, IV and V are thought to be involved in RNA binding. These are described more fully in the contribution by Linder (2,3). The accession numbers for these proteins are Dhx9- Q08211, Ddx20- Q9UH16, Ddx5- P17844, Ddx17- Q92841, Ddx21- Q9NR30 and Ddx54- Q8TDD1.