CAZyme Information: Bcin09g04150.1:RNA-p1

Basic Information

• Species: Botrytis cinerea
• Lineage: Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Botrytis; Botrytis cinerea
• CAZyme ID: Bcin09g04150.1:RNA-p1
• CAZy Family: GH43|CBM91
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
437		46019.03	5.8947

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BcinereaB05-10	12073	332648	366	11707

• Gene Location: location=bcin_chr_9:1465622-1466984(-)

Full Sequence      

MKCEKALDRMGSTKSHRSRKSSSMSRKLLAASICLAMLPIADAHTYYRNRATWKPNWDPN
RPVRKGPPKKRDGAIPLVVSNMCPETIWPGIGTQAGTGAGVGGFALQTGESKSLTVSADW
QGRIWGRTNCSFAVGGGGASNAAGNDGSGSACVTGDCGGLLDCSITGETPVTLAEFDLAG
NGGSQTFYDISLVDGYNIPMGIVYIPGDNPALQAIPPNLVNAACIASTGYLASPAVTGTN
GNSSNSTYPIPLEGKVTNDAAMSWCPWNLQKTPPDKPGDGVYPYPDDNIQRPTFDPCLSA
CAKDNKPSDCCTGAYDQPQLCPRNDFANAANAICPDAYGYPFDDQTSTFIIPTGGGWEIV
FCPVGRSTNILKVLGDQMRKIASAGKVTKDIIETAMNETYINEMAVKSTAGEGLSEKAKL
GSWGALVGVLVWGIWLC

Enzyme Prediction     

No EC number prediction in Bcin09g04150.1:RNA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	81	363	8.1e-58	0.9953703703703703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395248	Thaumatin	2.54e-88	81	363	1	211	Thaumatin family.
185757	TLP-PA	7.78e-57	81	362	6	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.
185754	Thaumatin-like	1.06e-55	77	362	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.
128501	THN	6.65e-48	79	363	3	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.
185756	TLP-P	3.95e-29	77	200	1	105	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSZ36549.1|GH152	2.83e-279	10	437	1	428
VBB73018.1|GH152	1.08e-139	75	428	121	473
QBZ65635.1|GH152	1.40e-136	75	401	9	333
UQC83697.1|GH152	2.09e-135	62	410	59	391
VDB89779.1|GH152	2.28e-133	26	383	726	1079

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZS3_A	6.14e-34	77	363	3	222	High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
2AHN_A	1.19e-32	81	363	7	222	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
4JRU_A	6.49e-28	79	363	5	201	Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera]
1DU5_A	7.13e-27	77	363	3	206	The Crystal Structure Of Zeamatin. [Zea mays],1DU5_B The Crystal Structure Of Zeamatin. [Zea mays]
1Z3Q_A	1.55e-25	79	363	5	200	Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7A [Musa acuminata]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P28493|PR5_ARATH	6.10e-46	74	363	23	239	Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1
sp|Q5DWG1|CRJ35_CRYJA	3.97e-42	71	363	19	238	Pathogenesis-related thaumatin-like protein 3.5 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|O80327|TLP1_PYRPY	1.31e-39	80	363	28	244	Thaumatin-like protein 1 OS=Pyrus pyrifolia OX=3767 GN=TL1 PE=1 SV=1
sp|P83332|TLP1_PRUPE	2.17e-34	74	363	24	246	Thaumatin-like protein 1 OS=Prunus persica OX=3760 PE=2 SV=1
sp|Q9FSG7|TP1A_MALDO	3.03e-33	74	363	24	246	Thaumatin-like protein 1a OS=Malus domestica OX=3750 GN=TL1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.166320	0.833662	CS pos: 43-44. Pr: 0.7283

TMHMM  Annotations     

There is no transmembrane helices in Bcin09g04150.1:RNA-p1.