CAZyme Information: KFA47865.1

Basic Information

• Species: Stachybotrys chartarum
• Lineage: Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
• CAZyme ID: KFA47865.1
• CAZy Family: AA9
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
412	KL651585|CGC1	44178.31	4.5125

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SchartarumIBT40293	11453	1280524	0	11453

• Gene Location: location=KL651585:126348-127639(-)

Full Sequence      

MRSSTRHRTASTTTSLGHLLAVLVSFGYLNGTAQAKDFPVASRNWQAAYLHQTKPGPPAK
RGPPPEDWDGRIPLLVTNGCDSTIWPGITSQAGTGPGVGGFELEAGEQRQLWVSPDWQGR
VWGRTNCTVDGDSCSCETGDCRGLLDCEFSGATPATLAEFTLAGGINGAQTFYDISLVDG
YNIPIGINYIPAENTTFIPPNLTNCACIATTGWLHDPATTGTYSTNSTYPVPLEDTGSNA
NIRNWCPWPYLVFPPTKPGDGIYPYPDDHIERPAFSPCNSACSATGSDRDCCVGDYHDPD
VCEPSAYSRSIKAICPDAYSFAFDDQQSTFIIPNGGGWEVVMCPTGRSTDILRQLGSEMN
ELANAGRLSDSAMRRLRDPTYIEADRGAGAEVRPVAKMVAVTALVVAVLLSV

Enzyme Prediction     

No EC number prediction in KFA47865.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	78	344	1.5e-69	0.9953703703703703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395248	Thaumatin	1.34e-92	78	344	1	211	Thaumatin family.
185757	TLP-PA	4.75e-57	76	343	4	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	1.68e-53	74	343	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	1.93e-49	76	344	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	2.20e-28	76	231	3	147	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
QPG96228.1|GH152	8.59e-209	16	394	1	378
QUC17904.1|GH152	1.30e-207	16	394	18	395
QLI69933.1|GH152	9.47e-203	15	394	105	483
UNI24053.1|GH152	7.51e-201	16	394	1	380
QKD55944.1|GH152	2.98e-196	1	412	1	411

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZS3_A	2.44e-39	74	344	3	222	High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
2AHN_A	8.00e-33	74	344	3	222	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
4L2J_A	1.45e-29	74	346	4	206	Crystal Structure of Osmotin, an antifungal laticifer protein [Calotropis procera]
4L5H_A	2.27e-29	76	344	5	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]
4JRU_A	9.12e-29	76	344	5	201	Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O80327|TLP1_PYRPY	2.48e-43	74	344	25	244	Thaumatin-like protein 1 OS=Pyrus pyrifolia OX=3767 GN=TL1 PE=1 SV=1
sp|Q5DWG1|CRJ35_CRYJA	4.62e-42	70	345	21	239	Pathogenesis-related thaumatin-like protein 3.5 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|P28493|PR5_ARATH	1.30e-40	74	344	26	239	Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1
sp|Q53MB8|TLPH_ORYSJ	1.90e-40	69	328	26	234	Thaumatin-like protein OS=Oryza sativa subsp. japonica OX=39947 GN=Os11g0706600 PE=2 SV=1
sp|Q9FSG7|TP1A_MALDO	2.41e-38	74	344	27	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
0.000544	0.999418	CS pos: 35-36. Pr: 0.9638

TMHMM  Annotations     

There is no transmembrane helices in KFA47865.1.