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Hydrophobin

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Fungal hydrophobin
Structure of hydrophobin HFBI from Trichoderma reesei
Identifiers
SymbolHydrophobin_2
PfamPF06766
InterProIPR010636
PROSITEPDOC00739
SCOP21r2m / SCOPe / SUPFAM
OPM protein1r2m
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1r2mB:17-82

Hydrophobins are a class of small, cysteine rich proteins (~ 100 amino acids) that are expressed only by filamentous fungi. They are known for their capability of forming a hydrophobic (water-repellent) coating on a surface of an object. They were first discovered and separated in Schizophyllum commune in 1991. Based on differences in hydropathy patterns and biophysical properties, they are divided into two categories: class I and class II.

Fungi make complex aerial structures and spores even in aqueous environments.

Hydrophobins have been identified in ascomycetes and basidiomycetes; whether they exist in other groups in not known.[1] Hydrophobins are generally found on the outer surface of conidia and of the hyphal wall, and may be involved in mediating contact and communication between the fungus and its environment.[2] Some family members contain multiple copies of the domain.

References

  1. ^ Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 11544369, please use {{cite journal}} with |pmid=11544369 instead.
  2. ^ Whiteford JR, Spanu PD (2001). "The hydrophobin HCf-1 of Cladosporium fulvum is required for efficient water-mediated dispersal of conidia". Fungal Genet. Biol. 32 (3): 159–168. doi:10.1006/fgbi.2001.1263. PMID 11343402.

Further reading