CAZyme Information: PHYBL_58313T0-p1

Basic Information

• Species: Phycomyces blakesleeanus
• Lineage: Mucoromycota; Mucoromycetes; ; Phycomycetaceae; Phycomyces; Phycomyces blakesleeanus
• CAZyme ID: PHYBL_58313T0-p1
• CAZy Family: GT2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
208		21145.01	3.6535

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PblakesleeanusNRRL1555	16528	763407	0	16528

• Gene Location: location=PblaNRRL1555-_SC02:613434-614060(-)

Full Sequence      

MYTSSAVVFCLAALAGLGSSAPTSGVTITVTNSCSYDVQVNQLTNDQTSNGDGSVLASGS
STDIQVASNWGGRIWARKECTGSTDCNASAPASLAEFLLNGANGDDFYDISLVDGYNVGM
SISPNGMSGSGQSCGTPTCSNLPACPTDAQVKDADGNVVGCESSCKDCDDSEYAAAVKAA
CPEAYSYSTDDSTSMYSCKATGYTVNLC

Enzyme Prediction     

No EC number prediction in PHYBL_58313T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	32	208	5.2e-35	0.9907407407407407

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395248	Thaumatin	6.67e-51	32	208	1	210	Thaumatin family.
185757	TLP-PA	1.00e-45	27	208	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	4.67e-35	28	208	1	217	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	1.77e-29	28	208	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.
185752	GH64-TLP-SF	4.21e-20	28	135	1	127	glycoside hydrolase family 64 (beta-1,3-glucanases which produce specific pentasaccharide oligomers) and thaumatin-like proteins. This superfamily includes glycoside hydrolases of family 64 (GH64), these are mostly bacterial beta-1,3-glucanases which cleave long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers and are implicated in fungal cell wall degradation. Also included in this superfamily are thaumatin, the sweet-tasting protein from the African berry Thaumatococcus daniellii, and thaumatin-like proteins (TLPs) which are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Like GH64s, some TLPs also hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. 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. Several members of the plant TLP family have been reported as food allergens from fruits, and pollen allergens from conifers. Streptomyces matensis laminaripentaose-producing, beta-1,3-glucanase (GH64-LPHase), and TLPs have in common, a core N-terminal barrel domain (domain I) composed of 10 beta-strands, two coming from the C-terminal region of the protein. In TLPs, this core domain is flanked by two shorter domains (domains II and III). Small TLPs, such as Triticum aestivum thaumatin-like xylanase inhibitor, have a deletion in the third domain (domain II). GH64-LPHase has a second C-terminal domain which corresponds positional to, but is much larger than, domain III of TLP. GH64-LPHase and TLPs are described as crescent-fold structures. Critical functional residues, common to GH64-LPHase and TLPs are a Glu and an Asp residue. LPHase has an electronegative, substrate-binding cleft and the afore mentioned conserved Glu and Asp residues are the catalytic residues essential for beta-1,3-glucan cleavage. In TLPs, these residues are two of the four conserved residues which contribute to the strong electronegative character of the cleft which is associated with the antifungal activity of TLPs.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHO46107.1|GH152	1.17e-33	27	208	27	248
QCE07013.1|GH152	2.89e-33	25	208	21	241
QCE07017.1|GH152	2.89e-33	25	208	21	241
BAX07474.1|GH152	2.95e-33	23	205	34	254
QHO46106.1|GH152	3.87e-33	27	208	27	248

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2AHN_A	2.10e-28	27	208	2	221	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
3ZS3_A	4.15e-28	28	208	3	221	High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
4JRU_A	6.29e-20	27	208	2	200	Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera]
1Z3Q_A	6.71e-18	27	208	2	199	Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7A [Musa acuminata]
1DU5_A	2.05e-17	51	208	21	205	The Crystal Structure Of Zeamatin. [Zea mays],1DU5_B The Crystal Structure Of Zeamatin. [Zea mays]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9SMH2|TLP1_CASSA	4.14e-29	28	208	25	242	Thaumatin-like protein 1 OS=Castanea sativa OX=21020 GN=TL1 PE=2 SV=1
sp|P83332|TLP1_PRUPE	6.24e-29	28	208	27	245	Thaumatin-like protein 1 OS=Prunus persica OX=3760 PE=2 SV=1
sp|P28493|PR5_ARATH	7.47e-29	23	208	16	238	Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1
sp|P50694|TLP_PRUAV	1.82e-27	27	208	25	244	Glucan endo-1,3-beta-glucosidase OS=Prunus avium OX=42229 PE=1 SV=1
sp|Q5DWG1|CRJ35_CRYJA	3.22e-27	24	208	20	237	Pathogenesis-related thaumatin-like protein 3.5 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
0.000227	0.999752	CS pos: 20-21. Pr: 0.9824

TMHMM  Annotations     

There is no transmembrane helices in PHYBL_58313T0-p1.