CAZyme Information: TRIREDRAFT_109835-t26_1-p1

Basic Information

• Species: Trichoderma reesei
• Lineage: Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma reesei
• CAZyme ID: TRIREDRAFT_109835-t26_1-p1
• CAZy Family: AA3
• CAZyme Description: predicted protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
354	GL985072|CGC3	38106.12	5.0128

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TreeseiQM6a	9138	431241	7	9131

• Gene Location: location=GL985072:526093-527280(-)

Full Sequence      

MNHNWQAVFFSENVNAPKGIKKRGPPGEAEERIPLVVTNKCESTIWPGVATQSGTGPGIG
RVWGRTNCTVNGESCACKTGDCFAKLDYEFSGATPATLAEFNLAGGVDNKQTFYDISLVD
GYNIPMGINYIPAKNTTFIPPNLTNCACIATAGWVYSAAGNGTFYSNATYPIPLESEETN
ESVSAWCPWLNLAFPPTEPGNGIYPYPDDNVQRPAFAPCNSACAATGSDKDCCIGKYHDP
NICKPSLYSKSVKAVCPDAYSFAFDDQTSTFIIPKGGGWEVVMCPEGRSTDILRKLGPEM
FELASGGKLSTLSLKRLQNATYVRAERGDAGLARPWVAMLVLGFVVAAYNWACL

Enzyme Prediction     

No EC number prediction in TRIREDRAFT_109835-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	60	285	1.8e-52	0.8009259259259259

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395248	Thaumatin	1.25e-72	39	285	1	211	Thaumatin family.
185757	TLP-PA	9.34e-41	37	284	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	1.86e-38	35	284	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	1.03e-34	37	285	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	1.03e-21	35	146	1	123	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	7.66e-197	5	346	30	392
UNI24053.1|GH152	1.93e-195	22	354	46	399
QUC17904.1|GH152	4.46e-193	5	335	47	395
QLI69933.1|GH152	5.72e-191	5	331	135	479
UKZ81149.1|GH152	2.51e-180	86	352	1	265

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZS3_A	8.58e-27	35	285	3	222	High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
1Z3Q_A	2.64e-25	37	285	5	200	Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7A [Musa acuminata]
1DU5_A	4.24e-25	35	285	3	206	The Crystal Structure Of Zeamatin. [Zea mays],1DU5_B The Crystal Structure Of Zeamatin. [Zea mays]
2AHN_A	6.17e-25	39	285	7	222	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
4L5H_A	9.33e-24	37	285	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1P8B554|THLP1_ARATH	6.94e-32	35	285	35	256	Thaumatin-like protein 1 OS=Arabidopsis thaliana OX=3702 GN=TLP1 PE=2 SV=1
sp|Q4W6C7|CRJ37_CRYJA	5.10e-30	39	285	34	231	Pathogenesis-related thaumatin-like protein 3.7 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|O80327|TLP1_PYRPY	3.74e-28	38	285	28	244	Thaumatin-like protein 1 OS=Pyrus pyrifolia OX=3767 GN=TL1 PE=1 SV=1
sp|Q5DWG1|CRJ35_CRYJA	3.44e-27	35	285	25	238	Pathogenesis-related thaumatin-like protein 3.5 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|P28493|PR5_ARATH	6.51e-27	35	285	26	239	Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999710	0.000317

TMHMM  Annotations     

There is no transmembrane helices in TRIREDRAFT_109835-t26_1-p1.