Fig. 2

Alignment of various DyP-type peroxidase sequences from P. sapidus (PsaDyP), P. ostreatus (PosDyP, NCBI: CAK55151), B. adusta (BadDyP, NCBI: BAA77283), A. auricula-judae (AauDyP, NCBI: AFJ79723) and M. scorodonius (MsP1, NCBI: BOBK71). Conserved amino acids (*); the characteristic GxxDG motif is enclosed in a frame; remnants of the H₂O₂ binding site (circle); E391 (blue); conserved residues of the heme binding site (gray background); potential heme binding residues (triangle); exposed amino acids of a potential LRET (long range electron transfer, green background); remnants involved in a potential LRET (green); N-terminal conserved amino acid sequences (white); conserved histidine residues (H164 and H166, blue background); signal sequences (gray); N-terminal amino acids are underlined