Figure 1

Platyhelminth DNMT candidates share extensive sequence similarity across the six conserved motifs and the target recognition domain (TRD) of DNA methyltransferase enzymes. A concatenated multiple sequence alignment of DNMT candidates from S. mansoni (Sm), S. japonicum (Sj), S. haematobium (Sh), C. sinensis (Cs), O. viverrini (Ov), F. hepatica (Fh) N. melleni (Nm), E. multilocularis (Em), E. granulosus (Eg), T. solium (Ts), H. microstoma (Hm), S. mediterranea (Smd) and M. lignano (Ml) with M. musculus DNMT2 and S. pombe PMT1 (NCBI accession numbers are listed in the Methods). The six highly conserved motifs in this catalytic domain are indicated above the alignment in Roman numerals (I, IV, VI, VIII, IX and X) as is the TRD. Numbers at the beginning of each motif represent amino acid positions and at each position the most conserved residues are further shaded in black, semi-conserved residues are highlighted grey and non-conserved amino acids are kept white. The row labelled 'consensus' represents the Pfam consensus sequence of the DNA methyltransferase (PF00145) domain where conserved amino acid residues (50–79%) are indicated by lower-case letters and highly conserved residues (> 80%) are indicated by upper-case letters. Functionally important cysteine (C), glutamic acid (E) and arginine (R) residues within motifs IV, VI and VIII respectively, are indicated by an asterisk (*) above the ‘consensus’ row. DNMT2 specific residues within the target recognition domain (TRD) are indicated by a plus (+) above the ‘consensus’ row. Missing amino acid residues, not present in truncated OvDNMT and NmDNMT candidates are indicated by a ‘N/A’.