Identification of a Classical Bipartite Nuclear Localization Signal in the Drosophila TEA/ATTS Protein Scalloped
Figure 1
Identification of a putative bipartite NLS.
(A) A schematic diagram of Sd. Sd contains two known functional domains, the TEA (DNA binding) domain and the Vestigial interacting domain (VID), as shown. At the C-terminus of the TEA domain, there is a 17 amino acid stretch from R145 to R161 which closely matches the consensus classic bipartite NLS sequence ([K/R]2[X]10[K/R]>3/5). (B) The region corresponding to the bipartite NLS shows strong identity with a variety of TEAD proteins from both animals and Choanozoa protists. Arrowheads mark the sites of the two N-terminal and five C-terminal residues known to be important for the classical bipartite sequence. ‘X’ marks the 10 intervening amino acids lying between the two termini. A ‘+’ indicates a basic residue (L/R) lies at one of the N- or C-terminal critical sites in the consensus sequence of the aligned TEAD proteins. The dark shading indicates identity with the consensus, while the lighter shading indicates similarity.