Chain A, Thaumatin I
Protein Classification
glycoside hydrolase 64/thaumatin family protein( domain architecture ID 545)
glycoside hydrolase 64 (GH64)/thaumatin family protein may be a beta-1,3-glucanase, a thaumatin, or a thaumatin-like protein (TLP) involved in host defense and a wide range of developmental processes
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| GH64-TLP-SF super family | cl02511 | glycoside hydrolase family 64 (beta-1,3-glucanases which produce specific pentasaccharide ... |
3-205 | 2.57e-106 | ||||
glycoside hydrolase family 64 (beta-1,3-glucanases which produce specific pentasaccharide oligomers) and thaumatin-like proteins; This superfamily includes glycoside hydrolases of family 64 (GH64), these are mostly bacterial beta-1,3-glucanases which cleave long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers and are implicated in fungal cell wall degradation. Also included in this superfamily are thaumatin, the sweet-tasting protein from the African berry Thaumatococcus daniellii, and thaumatin-like proteins (TLPs) which are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Like GH64s, some TLPs also hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. 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. Several members of the plant TLP family have been reported as food allergens from fruits, and pollen allergens from conifers. Streptomyces matensis laminaripentaose-producing, beta-1,3-glucanase (GH64-LPHase), and TLPs have in common, a core N-terminal barrel domain (domain I) composed of 10 beta-strands, two coming from the C-terminal region of the protein. In TLPs, this core domain is flanked by two shorter domains (domains II and III). Small TLPs, such as Triticum aestivum thaumatin-like xylanase inhibitor, have a deletion in the third domain (domain II). GH64-LPHase has a second C-terminal domain which corresponds positional to, but is much larger than, domain III of TLP. GH64-LPHase and TLPs are described as crescent-fold structures. Critical functional residues, common to GH64-LPHase and TLPs are a Glu and an Asp residue. LPHase has an electronegative, substrate-binding cleft and the afore mentioned conserved Glu and Asp residues are the catalytic residues essential for beta-1,3-glucan cleavage. In TLPs, these residues are two of the four conserved residues which contribute to the strong electronegative character of the cleft which is associated with the antifungal activity of TLPs. The actual alignment was detected with superfamily member smart00205: Pssm-ID: 470598 [Multi-domain] Cd Length: 218 Bit Score: 304.38 E-value: 2.57e-106
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| Name | Accession | Description | Interval | E-value | ||||
| THN | smart00205 | Thaumatin family; The thaumatin family gathers proteins related to plant pathogenesis. The ... |
3-205 | 2.57e-106 | ||||
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. Pssm-ID: 128501 [Multi-domain] Cd Length: 218 Bit Score: 304.38 E-value: 2.57e-106
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| TLP-P | cd09217 | thaumatin and allergenic/antifungal thaumatin-like proteins: plant homologs; This subfamily is ... |
3-205 | 4.02e-78 | ||||
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. Pssm-ID: 185756 Cd Length: 151 Bit Score: 230.74 E-value: 4.02e-78
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| Thaumatin | pfam00314 | Thaumatin family; |
7-205 | 4.97e-75 | ||||
Thaumatin family; Pssm-ID: 459757 Cd Length: 211 Bit Score: 224.76 E-value: 4.97e-75
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| Name | Accession | Description | Interval | E-value | ||||
| THN | smart00205 | Thaumatin family; The thaumatin family gathers proteins related to plant pathogenesis. The ... |
3-205 | 2.57e-106 | ||||
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. Pssm-ID: 128501 [Multi-domain] Cd Length: 218 Bit Score: 304.38 E-value: 2.57e-106
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| TLP-P | cd09217 | thaumatin and allergenic/antifungal thaumatin-like proteins: plant homologs; This subfamily is ... |
3-205 | 4.02e-78 | ||||
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. Pssm-ID: 185756 Cd Length: 151 Bit Score: 230.74 E-value: 4.02e-78
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| Thaumatin | pfam00314 | Thaumatin family; |
7-205 | 4.97e-75 | ||||
Thaumatin family; Pssm-ID: 459757 Cd Length: 211 Bit Score: 224.76 E-value: 4.97e-75
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| TLP-PA | cd09218 | allergenic/antifungal thaumatin-like proteins: plant and animal homologs; This subfamily is ... |
2-204 | 2.78e-67 | ||||
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. Pssm-ID: 185757 Cd Length: 219 Bit Score: 205.55 E-value: 2.78e-67
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| Thaumatin-like | cd09215 | the sweet-tasting protein, thaumatin, and thaumatin-like proteins involved in host defense; ... |
3-204 | 1.78e-45 | ||||
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. Pssm-ID: 185754 Cd Length: 157 Bit Score: 147.98 E-value: 1.78e-45
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| GH64-TLP-SF | cd08961 | glycoside hydrolase family 64 (beta-1,3-glucanases which produce specific pentasaccharide ... |
3-203 | 1.20e-37 | ||||
glycoside hydrolase family 64 (beta-1,3-glucanases which produce specific pentasaccharide oligomers) and thaumatin-like proteins; This superfamily includes glycoside hydrolases of family 64 (GH64), these are mostly bacterial beta-1,3-glucanases which cleave long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers and are implicated in fungal cell wall degradation. Also included in this superfamily are thaumatin, the sweet-tasting protein from the African berry Thaumatococcus daniellii, and thaumatin-like proteins (TLPs) which are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Like GH64s, some TLPs also hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. 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. Several members of the plant TLP family have been reported as food allergens from fruits, and pollen allergens from conifers. Streptomyces matensis laminaripentaose-producing, beta-1,3-glucanase (GH64-LPHase), and TLPs have in common, a core N-terminal barrel domain (domain I) composed of 10 beta-strands, two coming from the C-terminal region of the protein. In TLPs, this core domain is flanked by two shorter domains (domains II and III). Small TLPs, such as Triticum aestivum thaumatin-like xylanase inhibitor, have a deletion in the third domain (domain II). GH64-LPHase has a second C-terminal domain which corresponds positional to, but is much larger than, domain III of TLP. GH64-LPHase and TLPs are described as crescent-fold structures. Critical functional residues, common to GH64-LPHase and TLPs are a Glu and an Asp residue. LPHase has an electronegative, substrate-binding cleft and the afore mentioned conserved Glu and Asp residues are the catalytic residues essential for beta-1,3-glucan cleavage. In TLPs, these residues are two of the four conserved residues which contribute to the strong electronegative character of the cleft which is associated with the antifungal activity of TLPs. Pssm-ID: 185752 Cd Length: 153 Bit Score: 127.74 E-value: 1.20e-37
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| TLP-F | cd09219 | thaumatin-like proteins: basidiomycete homologs; This subfamily is represented by Lentinula ... |
3-205 | 7.41e-33 | ||||
thaumatin-like proteins: basidiomycete homologs; This subfamily is represented by Lentinula edodes TLG1, a thaumatin-like protein (TLP), as well as, other basidiomycete homologs. In general, TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. TLG1 TLP is involved in lentinan degradation and fruiting body senescence. TLG1 expressed in Escherichia coli and Aspergillus oryzae exhibited beta-1,3-glucanase activity and demonstrated lentinan degrading activity. TLG1 is proposed to be involved in lentinan and cell wall degradation during senescence following harvest and spore diffusion. TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. TLG1 from Lentinula edodes contains the required acidic amino acids conserved in the appropriate positions to possess an electronegative cleft. TLPs within this subfamily contain 13 conserved Cys residues; the number of total Cys residues in these TLPs varies from 16 in L. edodes TLG1 to 18 in other basidiomycete homologs. Pssm-ID: 185758 Cd Length: 229 Bit Score: 117.80 E-value: 7.41e-33
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| Blast search parameters | ||||
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