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Fig. 2 | Biotechnology for Biofuels

Fig. 2

From: Experimental recreation of the evolution of lignin-degrading enzymes from the Jurassic to date

Fig. 2

Alignment of the four most probable ancestral sequences (mature proteins) predicted with PAML 4.7 (using the WAG evolution model) and extant LiPH8 (alternative ancestral sequences are in Additional file 1: Fig. S1). Conserved catalytic and other relevant residues [24] are indicated including: two active site histidines (dark gray); three acidic residues forming the Mn2+-binding site (red); other active site conserved residues (light gray); one tryptophan involved in lignin direct oxidation (cyan); nine ligands of two Ca2+ ions (green); and eight cysteines forming disulfide bonds (yellow). Symbols below indicate full conservation of the same (asterisk) or equivalent residues (colon) and partial residue conservation (dot). The identity between the sequences decreased in the order: 87% (301) for AVP/ALiP, 86% (289) for CaPo/CaCD, 74% (257) for CaCD/ALiP, 74% (248) for CaPo/AVP, 72% (248) for ALiP/LiPH8, 70% (242) for CaPo/ALiP, 66% (226) for AVP/LiPH8, 61% (211) for CaCD/LiPH8, and 61% (209) for CaPo/LiPH8 (with the number of aligned residue pairs in parenthesis)

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