Figure 3. Sequence alignments from deduced hydrophobin protein sequences found in databases. Clustal W (1.82)  was used to align HCF-5 of Cladosporium fulvum (accession AJ133703), HCF-6 of Cladosporium fulvum (AJ251294), CU of Ophiostoma ulmi (U00963), CRP of Cryphonectria parasitica (L09559), CFTH1_I-III of Claviceps fusiformis (AJ133774), CPPH1_I-V of Claviceps purpurea (AJ418045), QID3 of Trichoderma harzianum (X71913), HFBI of Trichoderma reesei (Z68124), HFBII of Trichoderma reesei (Y11894), SRH1 of Trichoderma harzianum (Y11841), HFBIII of Trichoderma reesei (Nakari-Setälä, T., unpublished data), HYD5 of Gibberella moniliformis (AY158024), NCU08192.1 of Neurospora crassa (AABX01000408), MHP1 of Magnaporthe grisea (AF126872), HYD4 of Gibberella moniliformis (AY155499), XEH1 of Xanthoria ectaneoides (AJ250793), XPH1 of Xanthoria parietina (AJ250794), HCH-1 of Cladosporium herbarum (AJ496190), HCF-3 of Cladosporium fulvum (AJ566186), HCF-1 of Cladosporium fulvum (X98578), HCF-2 of Cladosporium fulvum (AJ133700), HCF-4 of Cladosporium fulvum (AJ566187), RODA of Emericella nidulans (M61113), HYP1/RODA of Aspergillus fumigatus (L25258, U06121), ROLA of Aspergillus oryzae (AB094496), RODB of Aspergillus fumigatus (AY057385), PbHYD2 of Paracoccidioides brasiliensis (AY427793), HYD1 of Gibberella moniliformis (AY155496), HYD2 of Gibberella moniliformis (AY155497), SSGA of Metarhizium anisopliae (M85281), MPG1 of Magnaporthe grisea (L20685), DEWA of Emericella nidulans (U07935), HYPB of Aspergillus fumigatus (AB097448), PbHYD1 of Paracoccidioides brasiliensis (AF526275), HYD3 of Gibberella moniliformis (AY155498), EAS of Neurospora crassa (AAB24462, X67339), POH2 of Pleurotus ostreatus (Y14657), COH1 of Coprinus cinereus (Y10627), DGH3 of Dictyonema glabratum (AJ320546), DGH2 of Dictyonema glabratum (AJ320545), DGH1 of Dictyonema glabratum (AJ320544), COH2 of Coprinus cinereus (Y10628), FVH1 of Flammulina velutipes (AB026720), Le.HYD1 of Lentinula edodes (AF217807), Le.HYD2 of Lentinula edodes (AF217808), SC3 of Schizophyllum commune (M32329), ABH3 of Agaricus bisporus (Y14602), POH3 of Pleurotus ostreatus (Y16881), FvHYD1 of Flammulina velutipes (AB126686), AF331452 of Pleurotus ostreatus (AF331452), SC4 of Schizophyllum commune (M32330), SC1 of Schizophyllum commune (X00788), SC6 of Schizophyllum commune (AJ007504), VMH3 of Pleurotus ostreatus (AJ238148), HYPB of Agaricus bisporus (Y15940), HYDPt-1 of Pisolithus tinctorius (U29605), HYDPt-2 of Pisolithus tinctorius (U29606), HYDPt-3 of Pisolithus tinctorius (AF097516), HYD1 of Tricholoma terreum (AY048578), POH1 of Pleurotus ostreatus (Y14656), FBHI of Pleurotus ostreatus (AJ004883), PNH2 of Pholiota nameko (AB079129), PNH1 of Pholiota nameko (AB079128), PNH3 of Pholiota nameko (AB079130), HYPA/ABH1 of Agaricus bisporus (X89242, X92861), HYPC/ABH2 of Agaricus bisporus (X90818, X92860), AaPRI2 of Agrocybe aegerita (AF081493), VMH1 of Pleurotus ostreatus (AJ238147) using the Gonnet matrix series . The protein databases were searched for annotated hydrophobin sequences showing the typical Cys patterning and omitting protein fragments or sequence variants. Only sequences after the first Cys were used in the alignments due to high variations in the amino termini. The Cys residues were aligned to show the typical Cys-pattern. The trihydrophobin (CFTH1) of Claviceps fusiformis and the pentahydrophobin (CPPH1) of Claviceps purpurea have multiple homologous hydrophobin domains linked with Gly/Asn-rich regions. For the alignments these protein sequences were divided into single domains and marked with roman numerals according to their order starting from the amino terminus. Note that the shown HFBII sequence begins at position three. aSecondary structure elements and the residues forming the hydrophobic patch are obtained from the HFBII crystal structure . bEAS secondary structure elements are obtained from an NMR-study . In the consensus sequences the residues that are fully conserved are shown in upper case and residues that are conserved over 80% are in lower case. For the residue shadings similarity groups based on the Blosum62 distance matrix  were used. Residue similarities of 100%, 80% and 60% are shown with a black, grey and light grey background, respectively.