Sequence alignment between X. dendrorhous CYP51 and S. cerevisiae ERG11 proteins and prediction of structurally conserved motifs in CYP51. Amino acid alignment between the deduced CYP51 sequence from X. dendrorhous (Xd) strain UCD 67–385 and the S. cerevisiae (Sc) strain S288c ERG11 (lanosterol C14-demethylase) protein [Swiss Protein: P10614]. Amino acid differences with the same properties are denoted with a plus (+). Structural elements are highlighted with the name of the corresponding feature above them: possible transmembrane helix (underlined and italics), alpha helices (red and italics), beta-sheets (blue and italics), meander loop and Cys pocket (white highlighted in black). The asterisks (*) indicate the three totally conserved amino acids among cytochromes P450. Secondary structural elements were predicted with the CYP450 Engineering database , and the potential transmembrane region was predicted with TMpred .