CAZyme Information: PHYBL_6777T0-p1

Basic Information

• Species: Phycomyces blakesleeanus
• Lineage: Mucoromycota; Mucoromycetes; ; Phycomycetaceae; Phycomyces; Phycomyces blakesleeanus
• CAZyme ID: PHYBL_6777T0-p1
• CAZy Family: GT20
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
175	PblaNRRL1555-_SC11|CGC1	18637.62	4.2213

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-_SC11:586784-587308(-)

Full Sequence      

VGAGSSKTYTLSSNWQGRLWGRKDCFENCPMAGAASPASLAEFNFKAHAGMDFYDVSFVD
GFNLPMSISPINGNKQQSGDTAYSCGSPLCSAVPSCPSDLQVIEDGEVVGCQSACSKYGT
DEYCCAGAFNTPQTCSTNIYSKAVKETCPQVYSFAYDDNTSTYVCQASGYTITFC

Enzyme Prediction     

No EC number prediction in PHYBL_6777T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	3	175	4.6e-48	0.8611111111111112

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395248	Thaumatin	1.39e-65	3	175	28	210	Thaumatin family.
185757	TLP-PA	6.69e-60	2	175	33	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	2.96e-47	15	175	45	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	1.01e-23	3	175	32	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.
185758	TLP-F	1.04e-23	3	175	36	228	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QVD39613.1|GH152	1.68e-47	1	174	52	245
ABK94768.1|GH152	2.94e-47	4	175	61	246
BBM98649.1|GH152	6.24e-47	4	175	62	244
QHN97715.1|GH152	1.51e-46	3	175	8	190
QIB84897.1|GH152	1.57e-46	3	175	43	230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZS3_A	1.78e-42	5	175	37	221	High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
2AHN_A	2.52e-42	15	175	47	221	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
4JRU_A	9.52e-25	4	175	26	200	Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera]
1PCV_A	2.91e-24	18	175	44	204	Crystal structure of osmotin, a plant antifungal protein [Nicotiana tabacum],1PCV_B Crystal structure of osmotin, a plant antifungal protein [Nicotiana tabacum]
1DU5_A	3.23e-23	36	175	78	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|Q5DWG1|CRJ35_CRYJA	1.78e-48	4	175	58	237	Pathogenesis-related thaumatin-like protein 3.5 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|O80327|TLP1_PYRPY	4.65e-44	1	175	55	243	Thaumatin-like protein 1 OS=Pyrus pyrifolia OX=3767 GN=TL1 PE=1 SV=1
sp|P28493|PR5_ARATH	8.10e-44	4	175	58	238	Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1
sp|Q9SMH2|TLP1_CASSA	1.81e-43	5	175	59	242	Thaumatin-like protein 1 OS=Castanea sativa OX=21020 GN=TL1 PE=2 SV=1
sp|Q9FSG7|TP1A_MALDO	1.76e-41	5	175	61	245	Thaumatin-like protein 1a OS=Malus domestica OX=3750 GN=TL1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000064	0.000003

TMHMM  Annotations     

There is no transmembrane helices in PHYBL_6777T0-p1.