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CAZyme Information: POV95319.1

You are here: Home > Sequence: POV95319.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Puccinia striiformis
Lineage Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
CAZyme ID POV95319.1
CAZy Family AA3
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
517 PKSM01000423|CGC1 55711.13 7.5625
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Pstriiformis93TX-2 14629 N/A 0 14629
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.39:2 3.2.1.39:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH152 34 175 2.2e-45 0.6574074074074074
GH152 230 421 8.1e-44 0.8564814814814815

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395248 Thaumatin 1.60e-58 23 170 9 149
Thaumatin family.
185758 TLP-F 2.62e-49 243 421 52 229
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.
185757 TLP-PA 9.22e-46 21 171 12 159
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.
185757 TLP-PA 3.47e-38 225 420 35 219
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.
185754 Thaumatin-like 2.42e-36 20 141 10 126
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
6.71e-59 21 421 30 254
2.39e-56 21 421 32 260
4.17e-56 21 421 32 256
2.55e-55 2 421 12 258
2.55e-55 2 421 12 258

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.11e-26 21 170 13 160
High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
5.10e-25 41 170 30 160
High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
3.08e-18 61 159 43 134
Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera],4L5H_B Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera],4MBT_A Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera],4MBT_B Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera]
5.09e-18 60 176 48 155
Structure of VIL-thaumatin [Thaumatococcus daniellii]
1.25e-17 60 176 48 155
Thaumatin Before A High Dose X-Ray 'Burn' [Thaumatococcus daniellii],2BLU_A Thaumatin After A High Dose X-Ray 'Burn' [Thaumatococcus daniellii],2VHK_A Atomic resolution (0.94 A) structure of purified thaumatin I grown in sodium L-tartrate at 22C [Thaumatococcus daniellii],2WBZ_A 1.6 A Structure of Thaumatin Crystallized without Tartrate at 4 C [Thaumatococcus daniellii],3N02_A Thaumatic crystals grown in loops/micromounts [Thaumatococcus daniellii],3N03_A Thaumatin crystals grown from drops [Thaumatococcus daniellii],4AXU_A CRYSTAL STRUCTURE OF THAUMATIN FROM AN AUTO-HARVESTED CRYSTAL, control experiment [Thaumatococcus daniellii],5AMZ_A Crystal Structure of Thaumatin processed with the CrystalDirect automated mounting and cryo-cooling technology [Thaumatococcus daniellii],5AVG_A The 0.95 angstrom structure of thaumatin crystallized in high-strength agarose hydrogel [Thaumatococcus daniellii]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.99e-28 41 175 52 183
Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1
1.98e-26 21 170 36 180
Thaumatin-like protein 2 OS=Prunus persica OX=3760 PE=2 SV=1
3.60e-25 21 170 36 183
Glucan endo-1,3-beta-glucosidase OS=Prunus avium OX=42229 PE=1 SV=1
3.85e-24 36 171 53 189
Thaumatin-like protein OS=Oryza sativa subsp. japonica OX=39947 GN=Os11g0706600 PE=2 SV=1
4.52e-24 41 170 54 184
Thaumatin-like protein 1a OS=Malus domestica OX=3750 GN=TL1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000031 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in POV95319.1.