Class I hydrophobins are a unique family of fungal proteins that form a polymeric, water-repellent monolayer on the surface of structures such as spores and fruiting bodies. They form amyloid-like rodlets which have an underlying cross-beta amyloid structure. This subfamily includes the rodlet proteins of Neurospora crassa (gene eas) and Aspergillus nidulans (gene rodA). They are the main component of the hydrophobic sheath covering the surface of many fungal spores. The surface hydrophobicity is important for processes such as association of hyphae in reproductive structures, dispersal of aerial spores, and adhesion of pathogens to host structures. This subfamily also includes Schizophyllum commune fruiting body proteins and Agaricus bisporus hydrophobins.
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