Summary: Fungal hydrophobin
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This is the Wikipedia entry entitled "Hydrophobin". More...
Hydrophobin Edit Wikipedia article
| Hydrophobin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Hydrophobin | ||||||||
| Pfam | PF01185 | ||||||||
| InterPro | IPR001338 | ||||||||
| PROSITE | PDOC00739 | ||||||||
| SCOP | 1r2m | ||||||||
| SUPERFAMILY | 1r2m | ||||||||
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| Fungal hydrophobin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Structure of hydrophobin HFBI from Trichoderma reesei | |||||||||
| Identifiers | |||||||||
| Symbol | Hydrophobin_2 | ||||||||
| Pfam | PF06766 | ||||||||
| InterPro | IPR010636 | ||||||||
| PROSITE | PDOC00739 | ||||||||
| SCOP | 1r2m | ||||||||
| SUPERFAMILY | 1r2m | ||||||||
| OPM protein | 1r2m | ||||||||
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Hydrophobins are a group of small (~100 amino acids) cysteine-rich proteins that are expressed only by filamentous fungi. They are known for their ability to form a hydrophobic (water-repellent) coating on the surface of an object.[1] They were first discovered and separated in Schizophyllum commune in 1991.[2] Based on differences in hydropathy patterns and biophysical properties, they can be divided into two categories: class I and class II. Hydrophobins can self-assemble into a monolayer on hydrophobic:hydrophilic interfaces such as an water:air interface. Class I monolayer contains the same core structure as amyloid fibrils, and is positive to Congo red and thioflavin T. The monolayer formed by class I hydrophobins has a highly ordered structure, and can only be dissociated by concentrated trifluoroacetate or formic acid.
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 is not known.[3] 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.[4] Some family members contain multiple copies of the domain.
This family of proteins includes the rodlet proteins of Neurospora crassa (gene eas) and Emericella nidulans (gene rodA), these proteins are the main component of the hydrophobic sheath covering the surface of many fungal spores.[5][6]
[edit] References
- ^ Sunde M, Kwan AH, Templeton MD, Beever RE, Mackay JP (October 2008). "Structural analysis of hydrophobins". Micron 39 (7): 773–84. doi:10.1016/j.micron.2007.08.003. PMID 17875392.
- ^ Wessels J, De Vries O, Asgeirsdottir SA, Schuren F (1991). "Hydrophobin Genes Involved in Formation of Aerial Hyphae and Fruit Bodies in Schizophyllum.". Plant Cell 3 (8): 793–799. doi:10.1105/tpc.3.8.793. PMC 160046. PMID 12324614. //www.ncbi.nlm.nih.gov/pmc/articles/PMC160046/.
- ^ Wösten (2001). "Hydrophobins: multipurpose proteins". Annual review of microbiology 55: 625–646. doi:10.1146/annurev.micro.55.1.625. PMID 11544369.
- ^ 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.
- ^ Stringer MA, Dean RA, Sewall TC, Timberlake WE (July 1991). "Rodletless, a new Aspergillus developmental mutant induced by directed gene inactivation". Genes Dev. 5 (7): 1161–71. PMID 2065971.
- ^ Lauter FR, Russo VE, Yanofsky C (December 1992). "Developmental and light regulation of eas, the structural gene for the rodlet protein of Neurospora". Genes Dev. 6 (12A): 2373–81. PMID 1459459.
[edit] Further reading
- Scholtmeijer K (2000). Expression and engineering of hydrophobin genes (Ph.D. thesis). University of Groningen. http://irs.ub.rug.nl/ppn/240088549.
- Hakanpää J, Paananen A, Askolin S, Nakari-Setälä T, Parkkinen T, Penttilä M, Linder MB, Rouvinen J (January 2004). "Atomic resolution structure of the HFBII hydrophobin, a self-assembling amphiphile". J. Biol. Chem. 279 (1): 534–9. doi:10.1074/jbc.M309650200. PMID 14555650.
- Wösten HA, de Vocht ML (September 2000). "Hydrophobins, the fungal coat unravelled". Biochim. Biophys. Acta 1469 (2): 79–86. doi:10.1016/S0304-4157(00)00002-2. PMID 10998570.
- Aimanianda V, Bayry J, Bozza S, Kniemeyer O, Perruccio K, Elluru SR, Clavaud C, Paris S, Brakhage AA, Kaveri SV, Romani L, Latgé JP (August 2009). "Surface hydrophobin prevents immune recognition of airborne fungal spores". Nature 460 (7259): 1117–21. doi:10.1038/nature08264. PMID 19713928.
This article incorporates text from the public domain Pfam and InterPro IPR001338
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Fungal hydrophobin Provide feedback
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External database links
| PANDIT: | PF01185 |
| PROSITE: | PDOC00739 |
| Pseudofam: | PF01185 |
| SYSTERS: | Hydrophobin |
This tab holds annotation information from the InterPro database.
InterPro entry IPR001338
The surface of many fungal spores is covered by a hydrophobic sheath, the rodlet layer, whose main component is a protein known as the rodlet protein [PUBMED:2065971, PUBMED:1459459]. The rodlet proteins of Neurospora crassa (gene eas) and Emericella nidulans (gene rodA) are evolutionary related to proteins found in the cell wall of fruiting bodies of the mushroom Schizophyllum commune (Bracket fungus) [PUBMED:2401401]. Collectively, these low-molecular-weight, cysteine-rich (eight conserved cysteines), hydrophobic proteins, are known as hydrophobins.Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | fungal-type cell wall (GO:0009277) |
| Molecular function | structural constituent of cell wall (GO:0005199) |
Domain organisation
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| RP15 (98) |
RP35 (127) |
RP55 (156) |
RP75 (178) |
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| PP/heatmap | 1 | |||||||
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| Seed (69) |
Full (519) |
Representative proteomes | NCBI (496) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (98) |
RP35 (127) |
RP55 (156) |
RP75 (178) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Curation
| Seed source: | Prosite |
| Previous IDs: | none |
| Type: | Family |
| Author: | Finn RD, Bateman A |
| Number in seed: | 69 |
| Number in full: | 519 |
| Average length of the domain: | 81.40 aa |
| Average identity of full alignment: | 33 % |
| Average coverage of the sequence by the domain: | 62.51 % |
HMM information
| HMM build commands: |
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 82 | ||||||||||||
| Family (HMM) version: | 13 | ||||||||||||
| Download: | download the raw HMM for this family |
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