Fig. 1

Amino acid sequence alignment of TausLPMO9B and other LPMOs. The LPMOs include: MtLPMO9A (MYCTH_85556; UniProt ID, G2QNT0), MtLPMO9B (MYCTH_80312; UniProt ID, G2QCJ3), TtLPMO9E (PDB ID, 3EJA; Uniprot ID, D0VWZ9), NcLPMO9C (PDB ID, 4D7U; Uniprot ID, Q7SHI8) and NcLPMO9F (PDB ID, 4QI8; Uniprot ID, Q1K4Q1). Fully conserved residues appear as white letters on red background. Residues that are highly conserved and share similar physico-chemical properties appear as red letters in blue squares. Residues involved in shaping the copper site, including the copper-binding histidine brace, are marked with blue asterisks. The secondary structure features indicated above the sequences are based on the NcLPMO9C structure [69] [β-strands, arrows; α-helices, coils; turns, T]. The residue numbering applies to NcLPMO9C. Previously annotated regions of high sequence variability and with a dominating loop structure, named L2, L3, LS and LC [75], are indicated by red, blue, green and brown bars, respectively, below the sequences. The experimentally determined oxidative regioselectivities of the LPMOs (C1, C4, C1/C4) are indicated to the left. Digits and question marks below the sequence indicate cysteine residues involved in the formation of disulfide bridges; green digits apply to NcLPMO9C, purple digits mark the ones predicted for TausLPMO9B and purple question marks indicate additional cysteines in TausLPMO9B. ESPript was used to generate the figure [67]. The predicted N-glycosylation site is marked in an orange box