Figure 3

A multiple alignment of the PRELI/MSF1p' domain was constructed using T-Coffee [32] and realigning the sequences by parsing high-scoring pairs from PSI-BLAST search results. The PHD-secondary structure [15] is shown above the alignment with E representing a β strand (upper-case is for predictions with > 82% accuracy; lower-case denotes predictions with > 72% accuracy). The 100% consensus shown below the alignment was derived using the following amino-acid classes: h, hydrophobic (ALICVMYFW, yellow shading); l, the aliphatic subset of the hydrophobic class (ALIVMC, yellow shading); a, aromatic (FHWY, yellow shading); c, charged (DEHKR, pink letters); s, small (ACDGNPSTV, green letters) and p, polar (CDEHKNQRST, blue letters). The limits of the domains are indicated by the residue positions on each side (except for the unfinished genome of Cryptosporidium parvum). The numbers within the alignment are poorly conserved inserts that are not shown. The different families are shown on the right. The PRELI and Kisir subgroups contain stand-alone versions of the domain, whereas the CG9528 family comprises Sec14-like proteins with an amino-terminal PRELI and a carboxy-terminal GOLD domain. The sequences are denoted by their gene name followed by the species abbreviation and GenBank Identifier. At, Arabidopsis thaliana; Ce, Caenorhabditis elegans; Cpar, Cryptosporidium parvum; Dm, Drosophila melanogaster; Hs, Homo sapiens; Mm, Mus musculus; Sc, Saccharomyces cerevisiae; Sp, Schizosaccharomyces pombe.