Fig. 2

Leader region motifs and new core peptides. A Conserved features of largest clusters of known core peptides. Consensus sequences of core peptides are shown for clusters of precursors with more than 10 representatives. The consensus for the multiple alignment of each cluster was determined as described in "Material and Methods" section. Conserved positions that could be involved in the formation of ester or amide bonds are highlighted by red, and variants of the GG-motifs are highlighted by blue. The asterisk indicates that for cluster 2, the diversity of the core peptides is so high that only aspartates required to form lactam bonds are conserved throughout the alignment, whereas the positions of hydroxyl-containing amino acids (Thr and Ser) are not conserved. Gaps in the consensus sequence were removed for compactness. B Conserved features of leader regions. Consensus sequences of leader peptides are shown for largest clusters of precursors. Consensus for multiple alignment of each cluster was determined as described in “Material and Methods” section. Conserved positions corresponding to a putative alpha helix which is interacting with ATP-grasp are highlighted by green. The alpha helix indicated schematically above the consensuses according to its position in microviridin precursor [26]. C Conserved features of core peptides identified in this work. Consensus sequences of core peptides are shown for clusters of precursors with 5 or more representatives. Consensus for multiple alignment of each cluster was determined as described in “Material and Methods” section. Conserved positions that can be involved in formation of ester or amide bonds are highlighted by red, variants of GG-motifs are highlighted by blue; conserved cysteine that could be involved in formation of thioether bonds are highlighted by orange. Red brackets show an only potential ester bond for two core peptides. Multiple potential cores in core region are underlined. Gaps in the consensus sequence were removed for compactness