Extended Data Fig. 1: Sequence alignments of Pex2, Pex10, and Pex12 from different species.

All sequences were retrieved from Uniprot and aligned with the program MUSCLE⁶⁰, using the default parameters in JalView⁶¹. Amino acids were colored with ClustalX according to their properties. The degree of amino acid conservation is indicated by the intensity of the color. RFs are shown as round-cornered rectangles and TMs as cylinders, with boundaries according to the cryo-EM structure. The plug is shown in purple. Black lines indicate loops in RFs that interact with E2 enzymes; residues mutated in these loops are labeled by blue dots. Red triangles show Cys residues in RFs that were mutated. Orange dots highlight residues at the interface between RF10 and RF12. The N- and C-terminal Pex2 sequences shown with a yellow background were deleted in the T. thermophilus construct used for cryo-EM. The long isoform of Human PEX10 (UniProtKB – O60683-2) was used for sequence alignment.