CAZyme Information: I306_00441-t38_1-p1

Basic Information

• Species: Cryptococcus gattii VGI
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus gattii VGI
• CAZyme ID: I306_00441-t38_1-p1
• CAZy Family: AA5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
190		20173.97	7.0893

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CgattiiEJB2	6908	1296103	145	6763

• Gene Location: location=KN848559:393774-394592(-)

Full Sequence      

MPSLNHPFIPSITALFSLVLFLSTHALAVRQLTVSNKCSSSIYVAVGGKGGALTTIGGAA
QPAGWKQAPGDYRNNGRIWARTGCTLNGDTLDCVVGGCSGNTIKRQVFLVWAIPFKFTID
VNHMDSYDISIVDGYNLPMEITSSDPSCAKGSCGTETDILTQCDPSLVYPKNSDKIYSCN
SACGNLIQSP

Enzyme Prediction     

No EC number prediction in I306_00441-t38_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	36	186	2.2e-29	0.7222222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395248	Thaumatin	8.12e-27	36	183	1	149	Thaumatin family.
185758	TLP-F	3.10e-20	32	183	1	158	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	3.36e-19	31	183	1	158	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	2.16e-17	32	183	1	156	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	1.62e-16	32	181	1	141	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
KGB75788.2|GH152	5.44e-113	1	188	1	198
AAW44358.2|GH152	4.17e-104	1	188	1	198
AUB26138.1|GH152	4.01e-103	1	188	1	198
AFR96243.2|GH152	4.01e-103	1	188	1	198
UOH81800.1|GH152	8.60e-84	1	188	1	181

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2AHN_A	3.28e-11	75	183	48	160	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
1Z3Q_A	9.03e-11	34	183	5	143	Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7A [Musa acuminata]
2D8P_A	1.37e-10	34	183	5	149	Structure of HYPER-VIL-thaumatin [Thaumatococcus daniellii]
5YYP_A	1.89e-10	34	183	5	149	Structure K137A thaumatin [Thaumatococcus daniellii]
5X9M_A	1.89e-10	34	183	5	149	Structure of hyper-sweet thaumatin (D21N) [Thaumatococcus daniellii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1P8B554|THLP1_ARATH	1.18e-15	16	183	14	195	Thaumatin-like protein 1 OS=Arabidopsis thaliana OX=3702 GN=TLP1 PE=2 SV=1
sp|Q8H994|CRJ33_CRYJA	7.64e-14	25	183	18	170	Pathogenesis-related thaumatin-like protein 3.3 (Fragment) OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|P31110|TLP_ORYSJ	1.65e-13	33	180	30	166	Thaumatin-like protein OS=Oryza sativa subsp. japonica OX=39947 GN=Os12g0628600 PE=1 SV=1
sp|P50698|RST4_AVESA	3.85e-13	11	181	4	159	Thaumatin-like pathogenesis-related protein 4 OS=Avena sativa OX=4498 GN=RASTL-4 PE=2 SV=1
sp|Q5DWG0|CRJ36_CRYJA	9.10e-13	7	167	4	160	Pathogenesis-related thaumatin-like protein 3.6 (Fragment) OS=Cryptomeria japonica OX=3369 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000498	0.999475	CS pos: 28-29. Pr: 0.7718

TMHMM  Annotations     

Start	End
7	29