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Conserved domains on  [gi|568446136|ref|XP_006457847|]
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hydrophobin-1 [Agaricus bisporus var. bisporus H97]

Protein Classification

hydrophobin family protein( domain architecture ID 17787263)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hydrophobin_I cd23507
class I hydrophobins; Class I hydrophobins are a unique family of fungal proteins that form a ...
 31-107 1.09e-18

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: 73.56  E-value: 1.09e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568446136  31 QCDVGEIHCCDTQQTPDHTSAAA--SGLLGVPINLGAFLGFDCTPISVLGVGGNNCAAQPVCCTGNQFTALINaLDCSP 107
Cdd:cd23507    1 QCSTGTLQCCNSVQSASSPAAAAllGLLGIVLQDLTGLVGLTCSPITVVGVGGNSCSAQPVCCENNSFGGLIA-IGCTP 78
 
Name Accession Description Interval E-value
hydrophobin_I cd23507
class I hydrophobins; Class I hydrophobins are a unique family of fungal proteins that form a ...
 31-107 1.09e-18

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: 73.56  E-value: 1.09e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568446136  31 QCDVGEIHCCDTQQTPDHTSAAA--SGLLGVPINLGAFLGFDCTPISVLGVGGNNCAAQPVCCTGNQFTALINaLDCSP 107
Cdd:cd23507    1 QCSTGTLQCCNSVQSASSPAAAAllGLLGIVLQDLTGLVGLTCSPITVVGVGGNSCSAQPVCCENNSFGGLIA-IGCTP 78
Hydrophobin pfam01185
Fungal hydrophobin;
32-108 5.66e-17

Fungal hydrophobin;


Pssm-ID: 426107 [Multi-domain]  Cd Length: 79  Bit Score: 69.22  E-value: 5.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568446136   32 CDVGEIHCCDTQQTP-DHTSAAASGLLGVPIN-LGAFLGFDCTPISVLGVGGNN-CAAQPVCCTGNQFTALINaLDCSPV 108
Cdd:pfam01185   1 CNTGPVQCCNSVTKAgSPALAGLLGLLGIVLQdLTGLVGLTCSPISVIGVGGGNsCSAQPVCCENNSFNGLVN-LGCTPI 79
HYDRO smart00075
Hydrophobins;
32-102 1.83e-16

Hydrophobins;


Pssm-ID: 214505  Cd Length: 76  Bit Score: 67.89  E-value: 1.83e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568446136    32 CDVGEIHCCDTQQTPDHTSAAA-SGLLGVPIN-LGAFLGFDCTPISVLGVG-GNNCAAQPVCCTGNQFTALINA 102
Cdd:smart00075   1 CNTGPVQCCNSVQTASSSSAALlLGLLGGVLGaLSGLVGLNCSPISVIGVGgGNSCSAQTVCCQNNQFNGLINI 74
 
Name Accession Description Interval E-value
hydrophobin_I cd23507
class I hydrophobins; Class I hydrophobins are a unique family of fungal proteins that form a ...
 31-107 1.09e-18

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: 73.56  E-value: 1.09e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568446136  31 QCDVGEIHCCDTQQTPDHTSAAA--SGLLGVPINLGAFLGFDCTPISVLGVGGNNCAAQPVCCTGNQFTALINaLDCSP 107
Cdd:cd23507    1 QCSTGTLQCCNSVQSASSPAAAAllGLLGIVLQDLTGLVGLTCSPITVVGVGGNSCSAQPVCCENNSFGGLIA-IGCTP 78
Hydrophobin pfam01185
Fungal hydrophobin;
32-108 5.66e-17

Fungal hydrophobin;


Pssm-ID: 426107 [Multi-domain]  Cd Length: 79  Bit Score: 69.22  E-value: 5.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568446136   32 CDVGEIHCCDTQQTP-DHTSAAASGLLGVPIN-LGAFLGFDCTPISVLGVGGNN-CAAQPVCCTGNQFTALINaLDCSPV 108
Cdd:pfam01185   1 CNTGPVQCCNSVTKAgSPALAGLLGLLGIVLQdLTGLVGLTCSPISVIGVGGGNsCSAQPVCCENNSFNGLVN-LGCTPI 79
HYDRO smart00075
Hydrophobins;
32-102 1.83e-16

Hydrophobins;


Pssm-ID: 214505  Cd Length: 76  Bit Score: 67.89  E-value: 1.83e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568446136    32 CDVGEIHCCDTQQTPDHTSAAA-SGLLGVPIN-LGAFLGFDCTPISVLGVG-GNNCAAQPVCCTGNQFTALINA 102
Cdd:smart00075   1 CNTGPVQCCNSVQTASSSSAALlLGLLGGVLGaLSGLVGLNCSPISVIGVGgGNSCSAQTVCCQNNQFNGLINI 74
hydrophobin cd23505
hydrophobins; Hydrophobins are a group of small cysteine-rich proteins that are expressed only ...
 32-103 3.43e-06

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: 41.67  E-value: 3.43e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568446136  32 CDVGEIHCCDTQQTPDHTSAAASGLLG--VPINLGAFLGFDCTPISVLGVGGNNCAAQPVCCTGNQFTALINAL 103
Cdd:cd23505    1 CSSGPVQCCATTVLGKHLDKGTTALLLniKIGDLKDLIGLDCSPPSVIGVFGNSCSAQAVCCVNPYQGGLQAIG 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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