Species | Pseudogymnoascus destructans | |||||||||||
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Lineage | Ascomycota; Leotiomycetes; ; Pseudeurotiaceae; Pseudogymnoascus; Pseudogymnoascus destructans | |||||||||||
CAZyme ID | ELR07965.1 | |||||||||||
CAZy Family | GH76 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH152 | 54 | 269 | 8.5e-47 | 0.8148148148148148 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
395248 | Thaumatin | 1.79e-53 | 54 | 277 | 1 | 180 | Thaumatin family. |
185754 | Thaumatin-like | 3.96e-48 | 50 | 182 | 1 | 130 | the sweet-tasting protein, thaumatin, and thaumatin-like proteins involved in host defense. This family is represented by the sweet-tasting protein thaumatin from the African berry Thaumatococcus daniellii and thaumatin-like proteins (TLPs) involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Plant TLPs are classified as pathogenesis-related (PR) protein family 5 (PR5), their expression is induced by environmental stresses such as pathogen/pest attack, drought and cold. TLPs included in this family are such proteins as zeamatin, found in high concentrations in cereal seeds; osmotin, a salt-induced protein in osmotically stressed plants; and PpAZ44, a propylene-induced TLP in abscission of young fruit. Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). Thaumatin and TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. Most TLPs contain 16 conserved Cys residues. A deletion within the third domain (domain II) of the Triticum aestivum thaumatin-like xylanase inhibitor is observed, thus, only 10 conserved Cys residues are present within this smaller TLP and similar homologs. |
185757 | TLP-PA | 1.36e-37 | 50 | 277 | 2 | 189 | allergenic/antifungal thaumatin-like proteins: plant and animal homologs. This subfamily is represented by the thaumatin-like proteins (TLPs), Cherry Allergen Pru Av 2 TLP, Peach PpAZ44 TLP (a propylene-induced TLP in abscission), the Caenorhabditis elegans thaumatin family member (thn-6), and other plant and animal homologs. TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Due to their inducible expression by environmental stresses such as pathogen/pest attack, drought and cold, plant TLPs are classified as the pathogenesis-related (PR) protein family 5 (PR5). Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. TLPs within this subfamily contain 16 conserved Cys residues. |
128501 | THN | 9.08e-31 | 50 | 268 | 1 | 178 | Thaumatin family. The thaumatin family gathers proteins related to plant pathogenesis. The thaumatin family includes very basic members with extracellular and vacuolar localization. Thaumatin itsel is a potent sweet-tasting protein. Several members of this family display significant in vitro activity of inhibiting hyphal growth or spore germination of various fungi probably by a membrane permeabilizing mechanism. |
185756 | TLP-P | 1.89e-25 | 50 | 160 | 1 | 102 | thaumatin and allergenic/antifungal thaumatin-like proteins: plant homologs. This subfamily is represented by the sweet-tasting protein thaumatin from the African berry Thaumatococcus daniellii, allergenic/antifungal Thaumatin-like proteins (TLPs), and related plant proteins. TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Plant TLPs are classified as pathogenesis-related (PR) protein family 5 (PR5), their expression is induced by environmental stresses such as pathogen/pest attack, drought and cold. TLPs in this subfamily include such proteins as zeamatin, found in high concentrations in cereal seeds, and osmotin, a salt-induced protein in osmotically stressed plants. Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). Thaumatin and TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. IgE-binding epitopes of mountain Cedar (Juniperus ashei) allergen Jun a 3, which interact with pooled IgE from patients suffering allergenic response to this allergen, were mainly located on the helical domain II; the best-conserved IgE-binding epitope predicted for TLPs corresponds to this region. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. Most TLPs contain 16 conserved Cys residues. A deletion within the third domain (domain II) of the Triticum aestivum thaumatin-like xylanase inhibitor is observed, thus, only 10 conserved Cys residues are present within this smaller TLP and similar homologs. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
5.77e-78 | 48 | 276 | 9 | 263 | |
1.76e-73 | 45 | 276 | 70 | 313 | |
3.51e-73 | 45 | 276 | 70 | 313 | |
3.51e-73 | 45 | 276 | 70 | 313 | |
1.32e-72 | 48 | 276 | 71 | 311 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.35e-27 | 50 | 268 | 3 | 182 | High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica] |
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1.06e-25 | 50 | 268 | 3 | 182 | High resolution structure of a cherry allergen Pru av 2 [Prunus avium] |
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2.17e-22 | 50 | 164 | 3 | 109 | Crystal structure of osmotin, a plant antifungal protein [Nicotiana tabacum],1PCV_B Crystal structure of osmotin, a plant antifungal protein [Nicotiana tabacum] |
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2.27e-22 | 50 | 164 | 3 | 109 | Chain A, Protein NP24 [Solanum lycopersicum] |
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1.04e-21 | 51 | 164 | 4 | 108 | Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.75e-28 | 47 | 163 | 32 | 154 | Thaumatin-like protein 1 OS=Arabidopsis thaliana OX=3702 GN=TLP1 PE=2 SV=1 |
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1.20e-26 | 50 | 268 | 27 | 206 | Thaumatin-like protein 1a OS=Malus domestica OX=3750 GN=TL1 PE=1 SV=1 |
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3.04e-26 | 26 | 161 | 8 | 125 | Pathogenesis-related protein 1A/1B OS=Hordeum vulgare OX=4513 PE=2 SV=1 |
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3.04e-26 | 26 | 161 | 8 | 125 | Pathogenesis-related protein 1C OS=Hordeum vulgare OX=4513 PE=2 SV=1 |
|
6.00e-26 | 38 | 165 | 19 | 139 | Thaumatin-like protein 1 OS=Castanea sativa OX=21020 GN=TL1 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.002764 | 0.997188 | CS pos: 44-45. Pr: 0.9117 |
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