CAZyme Information: PGTG_00963-t26_1-p1

Basic Information

• Species: Puccinia graminis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia graminis
• CAZyme ID: PGTG_00963-t26_1-p1
• CAZy Family: AA3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
184		19524.08	9.1214

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PgraminisCRL75-36-700-3	16309	418459	509	15800

• Gene Location: location=DS178264:990604-991462(-)

Full Sequence      

MLKAAVIIALLSSSILAVVVNGYTLHFKNNCKFPVWPAVGKAPNGQPDPSVSYGTKLNPG
GESQFGVNDREIGIRSWGRTGCDPKGANCATGACRGGLRCNEGRITSRVLLGEYGYQSFG
NVISWDLSRVDGSINIDTSINNGGNAKTCRKNNCPSNQAFAKPNDFQAITTSPVGSTFRI
TFCA

Enzyme Prediction     

No EC number prediction in PGTG_00963-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	29	169	1.3e-20	0.6435185185185185

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185754	Thaumatin-like	5.70e-22	25	183	1	157	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.
185756	TLP-P	8.81e-21	28	183	4	150	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.
185757	TLP-PA	8.86e-19	24	157	1	133	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	2.75e-17	27	174	3	149	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.
395248	Thaumatin	2.87e-17	29	157	1	124	Thaumatin family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VWO97639.1|GH152	4.69e-60	8	183	4	177
QRG28800.1|GH152	7.19e-14	24	183	22	172
QLF99121.1|GH152	7.19e-14	24	183	22	172
QLF99123.1|GH152	7.19e-14	24	183	22	172
QLF99122.1|GH152	7.19e-14	24	183	22	172

PDB Hits     

PGTG_00963-t26_1-p1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P27357|TLP_WHEAT	1.28e-14	24	183	22	172	Thaumatin-like protein PWIR2 OS=Triticum aestivum OX=4565 PE=2 SV=1
sp|P32938|PR1C_HORVU	3.63e-13	24	183	22	172	Pathogenesis-related protein 1C OS=Hordeum vulgare OX=4513 PE=2 SV=1
sp|P32937|PR1A_HORVU	1.37e-12	24	183	22	172	Pathogenesis-related protein 1A/1B OS=Hordeum vulgare OX=4513 PE=2 SV=1
sp|P83335|TLP2_PRUPE	5.54e-08	24	169	25	167	Thaumatin-like protein 2 OS=Prunus persica OX=3760 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000209	0.999768	CS pos: 22-23. Pr: 0.9762

TMHMM  Annotations     

Start	End
5	27