CAZyme Information: PTTG_04779-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_04779-t43_1-p1
• CAZy Family: GH27
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
252		26777.61	5.6485

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=ADAS02000024.1:830766-832162(-)

Full Sequence      

MKQAFVFIAQLFLASSIAARTFTIKNNCPFTIWPAHFTNPDSPARLTSQPAGWEAQQSSQ
KSFQVPDGWAGRFWGRRNCDFSKPGPTSCATGGCNGGLVCDSNTGSGVPPATLAEFKLNG
DGGKDYYDVSNVDGSNLPVLISNNKGCPSPSCGKDLNPGCPDDRLKVRDGNGVTIGCLSA
CQANLDGNHGDSANCCTGSHNTPATCPKDGVQYYNFFKGNCPDAYAYAYDESSQSALWTC
NQPADYTVTFCP

Enzyme Prediction     

EC	3.2.1.39:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	26	252	5.6e-72	0.9953703703703703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395248	Thaumatin	7.69e-101	26	252	1	211	Thaumatin family.
185758	TLP-F	2.39e-87	22	252	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	3.05e-79	21	251	1	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	6.63e-61	22	252	1	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	2.08e-50	22	251	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANC28050.1|GH152	5.51e-111	11	252	9	254
QRW16658.1|GH152	1.32e-105	13	252	10	260
ALA44968.1|GH152	1.02e-104	13	252	12	248
BAE95855.1|GH152|3.2.1.39	2.17e-104	18	252	20	258
BAE95856.1|GH152|3.2.1.39	2.17e-104	18	252	20	258

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZS3_A	4.29e-56	23	252	4	222	High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
2AHN_A	5.52e-54	21	252	2	222	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
4L5H_A	1.07e-35	21	252	2	198	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]
1DU5_A	6.30e-33	22	252	3	206	The Crystal Structure Of Zeamatin. [Zea mays],1DU5_B The Crystal Structure Of Zeamatin. [Zea mays]
4L2J_A	8.86e-33	21	252	3	204	Crystal Structure of Osmotin, an antifungal laticifer protein [Calotropis procera]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9FSG7|TP1A_MALDO	2.84e-56	8	252	14	246	Thaumatin-like protein 1a OS=Malus domestica OX=3750 GN=TL1 PE=1 SV=1
sp|P28493|PR5_ARATH	1.30e-55	11	252	13	239	Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1
sp|P50694|TLP_PRUAV	1.99e-53	19	252	23	245	Glucan endo-1,3-beta-glucosidase OS=Prunus avium OX=42229 PE=1 SV=1
sp|O80327|TLP1_PYRPY	3.08e-52	3	252	4	244	Thaumatin-like protein 1 OS=Pyrus pyrifolia OX=3767 GN=TL1 PE=1 SV=1
sp|P83335|TLP2_PRUPE	5.81e-52	19	252	23	242	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
0.000243	0.999714	CS pos: 19-20. Pr: 0.9490

TMHMM  Annotations     

There is no transmembrane helices in PTTG_04779-t43_1-p1.