Difference between revisions of "Part:BBa K4365027"

 
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The sequences of the hydrophobic signal peptide was collected from literature <ref>de Vocht ML et al (1998) Structural characterization of the hydrophobin SC3, as a monomer and after self-assembly at hydrophobic/hydrophilic interfaces, Biophys J.;74(4):2059-68. doi: 10.1016/s0006-3495(98)77912-3. PMID: 9545064; PMCID: PMC1299546.</ref> and was extracted via analysis of their sequence using the SignalP - 5.0 signal peptide predictor tool <ref name="signalp" />.
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Latest revision as of 14:09, 12 October 2022

Signal peptide of HCF-2 from Cladosporium fulvum

HCF-2 is a protein found in Cladosporium fulvum and belongs to a family of highly secreted proteins called hydrophobins.

Collection of fungal signal peptides
ID Source Species Prediction coefficient [1] turboRFP secretion
sp1 BBa_K4365006 MPGI Magnaporthe grisea 0.9562 Yes
sp2 BBa_K4365007 RodA Aspergillus nidulans 0.9553 Yes
sp3 BBa_K4365008 HYPI Aspergillus fumigatus 0.9703 No
sp4 BBa_K4365009 SsgA Metarhizium anisopliae 0.9126 No
sp5 BBa_K4365010 HCF-4 Cladosporium fulvum 0.9126 Yes
sp6 BBa_K4365025 HCF-5 Cladosporium fulvum 0.9234 NA
sp7 BBa_K4365026 CCG-2 Neurospora crassa 0.9566 NA
sp8 BBa_K4365011 HCF-1 Cladosporium fulvum 0.6850 Yes
sp9 BBa_K4365027 HCF-2 Cladosporium fulvum 0.8144 NA
sp10 BBa_K4365012 HCF-3 Cladosporium fulvum 0.7934 No
sp11 BBa_K4365013 SC3 Schizophyllum commune 0.6327 No
sp12 BBa_K4365014 ABH3 Agaricus bisporus 0.9458 Yes
sp13 BBa_K4365028 COH1 Coprinus cinereus 0.8545 NA
sp14 BBa_K4365015 FBH1 Pleurotus ostreatus 0.3367 Yes
sp15 BBa_K4365016 Aa-PRI2 Agrocybe aegerita 0.6356 Yes
sp16 BBa_K4365033 Hyd-Pt1 Pisolithus tinctorius 0.8352 NA
sp17 BBa_K4365017 HFBI Trichoderma reesei 0.9851 Yes
sp18 BBa_K4365018 HFBII Trichoderma reesei 0.6862 Yes
sp19 BBa_K4365019 α-mating factor Saccharomyces cerevisiae 0.9988 Yes


The sequences of the hydrophobic signal peptide was collected from literature [2] and was extracted via analysis of their sequence using the SignalP - 5.0 signal peptide predictor tool [1].

  1. 1.0 1.1 José Juan Almagro Armenteros et al. (2019) SignalP 5.0 improves signal peptide predictions using deep neural networks Nature Biotechnology, 37, 420-423, doi: 10.1038/s41587-019-0036-z
  2. de Vocht ML et al (1998) Structural characterization of the hydrophobin SC3, as a monomer and after self-assembly at hydrophobic/hydrophilic interfaces, Biophys J.;74(4):2059-68. doi: 10.1016/s0006-3495(98)77912-3. PMID: 9545064; PMCID: PMC1299546.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]