Figure 3. Structure-based sequence alignment of the helicase C domains of the SF2 helicases UvrB (2D7D), Hel308 (2P6R), RecG (1GM5), and TRCF (2EYQ).

Their consensus secondary structure elements are shown bellow as red spirals (α-helices) and blue arrows (β-strands). The sequence alignment of KIAA0415 obtained from threading and used to build a 3D model of its putative helicase C-like domain based on these structural templates is shown at the top. Sequence conservation of KIAA0415 with respect to the template structures is highlighted in grey (conservative) and yellow (semi-conservative). Gap deletions and insertions are represented by dashed lines and inverted U symbols, respectively. Insertions are labelled with the corresponding N- and C-ending residue numbering (black for KIAA0415, green for UvrB, and blue for Hel208). Regions I, Ia, II, III, IV, and V of consensus SF2 helicase motifs are underlined. Residues involved in ADP- and Mg²⁺ binding are coloured in blue and red, respectively.