CAZyme Information: PTTG_05907-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_05907-t43_1-p1
• CAZy Family: GH47
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
183		19181.38	8.2989

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ptriticina1-1BBBDRace1	15692	630390	814	14878

• Gene Location: location=ADAS02000014.1:698324-699113(+)

Full Sequence      

MFKSAVITALLGSNLGVAVQGYTLHFQNKCNFAVWPAVGKAVNGQPDPSVSYGAKLNPGG
ASRFSVHDREIGIRSWGRTGCDANGANCATGACRGGLRCDDGGITSRVLLGEYGYQSFGN
VISWDLSRVDGSININTSITNGGNTKTCRQNNCPSNQAFAQPNDFQAITTSPVGSTFSIT
FCA

Enzyme Prediction     

No EC number prediction in PTTG_05907-t43_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	28	169	1.1e-20	0.6481481481481481

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185754	Thaumatin-like	1.08e-20	24	182	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	3.36e-19	28	182	5	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	3.46e-19	23	156	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	1.71e-17	26	173	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	5.74e-17	28	156	1	124	Thaumatin family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VWO97639.1|GH152	1.83e-59	7	182	4	177
CDR37931.1|GH152	4.38e-13	3	154	13	158
QRG28800.1|GH152	1.99e-12	1	182	1	172
QLF99121.1|GH152	1.99e-12	1	182	1	172
QLF99123.1|GH152	1.99e-12	1	182	1	172

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BCT_A	1.46e-09	23	167	2	136	Crystal structure of kiwi-fruit allergen Act d 2 [Actinidia deliciosa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P27357|TLP_WHEAT	3.54e-13	1	182	1	172	Thaumatin-like protein PWIR2 OS=Triticum aestivum OX=4565 PE=2 SV=1
sp|P32937|PR1A_HORVU	1.87e-12	1	182	1	172	Pathogenesis-related protein 1A/1B OS=Hordeum vulgare OX=4513 PE=2 SV=1
sp|P32938|PR1C_HORVU	1.87e-12	1	182	1	172	Pathogenesis-related protein 1C OS=Hordeum vulgare OX=4513 PE=2 SV=1
sp|P83958|TLP_ACTCC	3.06e-12	2	167	4	160	Thaumatin-like protein OS=Actinidia chinensis var. chinensis OX=1590841 GN=TLP PE=1 SV=2
sp|P81370|TLP_ACTDE	2.99e-11	2	167	4	160	Thaumatin-like protein OS=Actinidia deliciosa OX=3627 GN=tlp PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.223245	0.776721	CS pos: 21-22. Pr: 0.6061

TMHMM  Annotations     

There is no transmembrane helices in PTTG_05907-t43_1-p1.