Figure 1

Multiple sequence alignment of DCD-domains. The alignment was built using T-coffee [21] and refined manually. First column: database accession numbers (Genbank, if available); second column: species names (at: Arabidopsis thaliana; cp: Citrus X paradisi; cr: Ceratopteris richardii; gm: Glycine max; mt: Medicago truncatula; os: Oryza sativa; tp: Thalassiosira pseudonana); third column: start of the domain in the respective sequences. The aligment is coloured by chroma [22]. (conserved prolines: white on grey; conserved glycines and alanines: green on grey; conserved leucines, isoleucines, phenylalanines, cysteines, valines and tyrosines: yellow on grey; conserved asparagines and glutamines: dark red on grey; conserved glutamic acids: light red on grey; conserved threonines and serines: light blue on grey; conserved aliphatic residues: grey on yellow; conserved hydrophobic residues: black on yellow; conserved small residues: dark green on white; conserved positively charged residues: blue on white; conserved polar residues: dark blue on white; conserved charged residues: pink on white; conserved aromatic residues: blue on yellow; conserved big residues: blue on light yellow; conserved negatively charged residues: red on white) The consensus sequence (conserved in 80% of the sequences) shown below; h, p, s, l, b, c, a, + and – indicate hydrophobic, polar, small, aliphatic, big, charged, aromatic, positively charged and negatively charged residues, respectively. The predicted secondary structure taken from the consensus of the alignment (H, helix or E, beta sheet predicted with expected average accuracy > 82%; h, helix or e, beta sheet predicted with expected average accuracy < 82%) using PhD [23]. Independent predictions have been performed for Psipred 17 using representatives of distinct groups (accession number: gi|2369766, gi|50932255, gi|51535545). Asterisks on the top of the alignment indicate conserved Cystein residues (red: present in almost all DCD domains, green: present subfamily-specific)