hypothetical protein JAAARDRAFT_195498 [Jaapia argillacea MUCL 33604]
Protein Classification
hydrophobin family protein( domain architecture ID 10471864)
fungal hydrophobin family protein similar to Aspergillus fumigatus hydrophobin Hyp1/RodA, which is a cell wall protein regularly arranged in interwoven fascicules of clustered proteinaceous microfibrils, or rodlets, to form the outer spore coat protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Hydrophobin | pfam01185 | Fungal hydrophobin; |
43-121 | 9.38e-29 | ||
Fungal hydrophobin; : Pssm-ID: 426107 [Multi-domain] Cd Length: 79 Bit Score: 99.65 E-value: 9.38e-29
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| Name | Accession | Description | Interval | E-value | ||
| Hydrophobin | pfam01185 | Fungal hydrophobin; |
43-121 | 9.38e-29 | ||
Fungal hydrophobin; Pssm-ID: 426107 [Multi-domain] Cd Length: 79 Bit Score: 99.65 E-value: 9.38e-29
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| hydrophobin_I | cd23507 | class I hydrophobins; Class I hydrophobins are a unique family of fungal proteins that form a ... |
42-120 | 1.17e-24 | ||
class I hydrophobins; 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. Pssm-ID: 438003 [Multi-domain] Cd Length: 78 Bit Score: 89.36 E-value: 1.17e-24
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| HYDRO | smart00075 | Hydrophobins; |
43-118 | 1.68e-17 | ||
Hydrophobins; Pssm-ID: 214505 Cd Length: 76 Bit Score: 70.98 E-value: 1.68e-17
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| Name | Accession | Description | Interval | E-value | ||
| Hydrophobin | pfam01185 | Fungal hydrophobin; |
43-121 | 9.38e-29 | ||
Fungal hydrophobin; Pssm-ID: 426107 [Multi-domain] Cd Length: 79 Bit Score: 99.65 E-value: 9.38e-29
|
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| hydrophobin_I | cd23507 | class I hydrophobins; Class I hydrophobins are a unique family of fungal proteins that form a ... |
42-120 | 1.17e-24 | ||
class I hydrophobins; 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. Pssm-ID: 438003 [Multi-domain] Cd Length: 78 Bit Score: 89.36 E-value: 1.17e-24
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| HYDRO | smart00075 | Hydrophobins; |
43-118 | 1.68e-17 | ||
Hydrophobins; Pssm-ID: 214505 Cd Length: 76 Bit Score: 70.98 E-value: 1.68e-17
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| hydrophobin | cd23505 | hydrophobins; Hydrophobins are a group of small cysteine-rich proteins that are expressed only ... |
43-120 | 1.03e-13 | ||
hydrophobins; Hydrophobins are a group of small cysteine-rich proteins that are expressed only by filamentous fungi and play important roles in fungal growth. They are characterized by the presence of 8 conserved cysteine residues that form 4 disulfide bonds. They contribute to surface hydrophobicity, which is important for processes such as association of hyphae in reproductive structures, dispersal of aerial spores and adhesion of pathogens to host structures. Hydrophobins have been divided into two classes based on their hydropathy patterns and biophysical properties. A key difference between class I and class II hydrophobins is that only class I hydrophobins form amyloid-like rodlets which have an underlying cross-beta amyloid structure. Class II hydrophobin films are significantly less robust and lack the rodlet morphology of class I hydrophobins. Pssm-ID: 438002 Cd Length: 77 Bit Score: 61.31 E-value: 1.03e-13
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