CAZyme Information: OAG18632.1

Basic Information

• Species: Alternaria alternata
• Lineage: Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata
• CAZyme ID: OAG18632.1
• CAZy Family: GH13
• CAZyme Description: Osmotin, thaumatin-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
374		40685.50	4.8492

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AalternataSRC1lrK2f	13577	N/A	111	13466

• Gene Location: location=KV441483:556790-558014(+)

Full Sequence      

MAQKAPWKANRRKLDITPLLVTNRCPESIWPGISTQSGTGPGENGFKLEPGETKNQTVSE
DWQGRVWGRTNCTFNSDGTAAESGRGKACGSGDCNGALNCQVGGDVPVSLAEFTLDAGDG
HTYYDISLVDGYNVPMAIVLQPLENVTLDDIPPNLTNPSCQGTDGLLASQGYNPYPEYPD
FLRTNTSYPLPFDQKVDKNKISKWCPWDLQQNPPEKPGDGVYPYPDDNIQRPQFNPCFSA
CAKNNRPEDCCTGEYNSASACKPSEYSKNVKAVCPDAYSFAFDDQTSTFIIPSGAGFEVV
FCPGARSTTILSTSREEMLQLAQQGRVDKQATMMMKSKSEMAKRSAASRISKLGGNPFAF
VLVVVAVTSASHFW

Enzyme Prediction     

No EC number prediction in OAG18632.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	23	303	6.8e-62	0.9953703703703703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395248	Thaumatin	3.36e-97	23	303	1	211	Thaumatin family.
185754	Thaumatin-like	2.28e-67	19	302	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.
185757	TLP-PA	8.83e-63	21	302	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.
128501	THN	7.42e-51	21	303	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	1.29e-28	21	138	3	107	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
CAE7030729.1|GH152	3.69e-241	1	373	1	374
QRC92249.1|GH152	2.99e-224	1	348	41	388
CBX99479.1|GH152|GH2	6.88e-201	1	353	36	389
QDS77702.1|GH152	9.98e-158	2	312	48	359
QBZ65635.1|GH152	1.79e-128	18	327	10	319

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2AHN_A	4.15e-32	23	303	7	222	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
3ZS3_A	2.19e-31	22	303	6	222	High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
4L5H_A	1.69e-30	21	303	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]
1DU5_A	7.84e-30	21	303	5	206	The Crystal Structure Of Zeamatin. [Zea mays],1DU5_B The Crystal Structure Of Zeamatin. [Zea mays]
1Z3Q_A	9.53e-29	21	303	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|Q5DWG1|CRJ35_CRYJA	3.08e-45	17	305	23	240	Pathogenesis-related thaumatin-like protein 3.5 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|Q8H994|CRJ33_CRYJA	2.07e-42	21	302	29	229	Pathogenesis-related thaumatin-like protein 3.3 (Fragment) OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|P28493|PR5_ARATH	1.45e-41	17	303	24	239	Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1
sp|Q8H996|CRJ31_CRYJA	2.35e-41	21	302	31	231	Pathogenesis-related thaumatin-like protein 3.1 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|Q8H995|CRJ32_CRYJA	1.31e-40	21	302	32	232	Pathogenesis-related thaumatin-like protein 3.2 OS=Cryptomeria japonica OX=3369 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000036	0.000002

TMHMM  Annotations     

There is no transmembrane helices in OAG18632.1.