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CAZyme Information: CNBF4180-t26_1-p1

You are here: Home > Sequence: CNBF4180-t26_1-p1

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 Cryptococcus neoformans
Lineage Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus neoformans
CAZyme ID CNBF4180-t26_1-p1
CAZy Family GH37
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
457 47290.77 6.0724
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CneoformansB-3501A 6608 283643 108 6500
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.39:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH152 36 271 5.1e-50 0.9953703703703703

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395248 Thaumatin 3.40e-49 36 271 1 211
Thaumatin family.
185758 TLP-F 1.09e-36 32 271 1 229
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 4.90e-35 33 270 3 219
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.
128501 THN 1.42e-31 33 271 2 218
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.
185754 Thaumatin-like 2.43e-26 32 163 1 126
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
1.98e-314 1 457 1 465
1.84e-245 1 440 1 444
1.08e-244 1 421 1 430
1.08e-244 1 421 1 430
4.50e-223 1 421 1 431

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.17e-21 34 271 5 205
Structure of hyper-sweet thaumatin (D21N) [Thaumatococcus daniellii]
4.17e-21 34 271 5 205
Structure K137A thaumatin [Thaumatococcus daniellii]
4.17e-21 34 271 5 205
Structure K78A thaumatin [Thaumatococcus daniellii]
5.59e-21 34 271 5 205
Thaumatin solved by Native SAD from a dataset collected in 0.6 second with JUNGFRAU detector [Thaumatococcus daniellii]
5.71e-21 34 271 5 205
The Structures Of Three Crystal Forms Of The Sweet Protein Thaumatin [Thaumatococcus daniellii],2PE7_A Thaumatin from Thaumatococcus Danielli in complex with tris-dipicolinate Europium [Thaumatococcus daniellii],3AL7_A Recombinant thaumatin I at 1.1 A [Thaumatococcus daniellii],3ALD_A Crystal structure of sweet-tasting protein Thaumatin I at 1.10 A [Thaumatococcus daniellii],3E3S_A Structure of thaumatin with the magic triangle I3C [Thaumatococcus daniellii],3V7V_A Thaumatin by Classical Hanging Drop Vapour Diffusion after 1.81 MGy X-Ray dose at ESRF ID29 beamline (Best Case) [Thaumatococcus daniellii],3V82_A Thaumatin by LB based Hanging Drop Vapour Diffusion after 1.81 MGy X-Ray dose at ESRF ID29 beamline (Best Case) [Thaumatococcus daniellii],3V84_A Thaumatin by LB based Hanging Drop Vapour Diffusion after 1.81 MGy X-Ray dose at ESRF ID29 beamline (Worst Case) [Thaumatococcus daniellii],3V87_A Thaumatin by Classical Hanging Drop Vapour Diffusion after 1.81 MGy X-Ray dose at ESRF ID29 beamline (Worst Case) [Thaumatococcus daniellii],3V88_A Thaumatin by Classical Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Best Case) [Thaumatococcus daniellii],3V8A_A Thaumatin by Classical Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Worst Case) [Thaumatococcus daniellii],3VCE_A Thaumatin by LB based Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Best Case) [Thaumatococcus daniellii],3VCG_A Thaumatin by LB based Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Worst Case) [Thaumatococcus daniellii],3VCH_A Thaumatin by Classical Hanging Drop Vapour Diffusion after 9.05 MGy X-Ray dose at ESRF ID29 beamline (Best Case) [Thaumatococcus daniellii],3VCI_A Thaumatin by Classical Hanging Drop Vapour Diffusion after 9.05 MGy X-Ray dose at ESRF ID29 beamline (Worst Case) [Thaumatococcus daniellii],3VCJ_A Thaumatin by LB Hanging Drop Vapour Diffusion after 9.05 MGy X-Ray dose at ESRF ID29 beamline (Best Case) [Thaumatococcus daniellii],3VCK_A Thaumatin by LB Hanging Drop Vapour Diffusion after 9.05 MGy X-Ray dose at ESRF ID29 beamline (Worst Case) [Thaumatococcus daniellii],3VHF_A plant thaumatin I at pH 8.0 [Thaumatococcus daniellii],3VHG_A Recombinant thaumatin I at PH 8.0 [Thaumatococcus daniellii],3VJQ_A Recombinant thaumatin at pH 8.0 with hydrogen atoms [Thaumatococcus daniellii],3WXS_A Thaumatin structure determined by SPring-8 Angstrom Compact free electron Laser (SACLA) [Thaumatococcus daniellii],3X3O_A Recombinant thaumatin in the presence of 0.5M PST at 298K [Thaumatococcus daniellii],3X3P_A Recombinant thaumatin in the presence of 0.75M PST at 293K [Thaumatococcus daniellii],3X3Q_A Structure of recombinant thaumatin in the presence of 1.0M PST, pH7 at 293K [Thaumatococcus daniellii],3X3R_A Recombinant thaumatin in the presence of 1.0M PST and soaked 1 hr at 293K [Thaumatococcus daniellii],3X3S_A Recombinant thaumatin in the presence of 1.5M PST at 293K [Thaumatococcus daniellii],3X3T_A Recombinant thaumatin in the presence of 1.5M PST at 293K [Thaumatococcus daniellii],4DC5_A Crystal Structure of Thaumatin Unexposed to Excessive SONICC Imaging Laser Dose. [Thaumatococcus daniellii],4DC6_A Crystal Structure of Thaumatin Exposed to Excessive SONICC Imaging Laser Dose. [Thaumatococcus daniellii],4XVB_A Recombinant thaumatin in the presence of 1.5M PST at 293K [Thaumatococcus daniellii],5GQP_A Thaumatin Structure at pH 8.0, orthorhombic type1 [Thaumatococcus daniellii],5SW0_A Thaumatin Structure at pH 4.0 [Thaumatococcus daniellii],5SW1_A Thaumatin Structure at pH 6.0 [Thaumatococcus daniellii],5SW2_A Thaumatin Structure at pH 6.0, orthorhombic type1 [Thaumatococcus daniellii],5WR8_A Thaumatin structure determined by SACLA at 1.55 Angstrom [Thaumatococcus daniellii],5X9L_A Recombinant thaumatin I at 0.9 Angstrom [Thaumatococcus daniellii],6RVO_A Multicrystal dataset of thaumatin collected using a multilayer monochromator. [Thaumatococcus daniellii],7AT6_A Chain A, Thaumatin I [Thaumatococcus daniellii]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.00e-27 32 272 35 257
Thaumatin-like protein 1 OS=Arabidopsis thaliana OX=3702 GN=TLP1 PE=2 SV=1
3.91e-20 15 271 10 227
Thaumatin I OS=Thaumatococcus daniellii OX=4621 PE=1 SV=2
8.07e-20 33 272 26 239
Pathogenesis-related thaumatin-like protein 3.5 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
1.08e-19 8 271 3 239
Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1
1.60e-19 15 272 8 240
Thaumatin-like protein OS=Arabidopsis thaliana OX=3702 GN=At1g18250 PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.239751 0.760227 CS pos: 28-29. Pr: 0.7345

TMHMM  Annotations      download full data without filtering help

Start End
7 29