CAZyme Information: SMAC_12587-t26_1-p1

Basic Information

• Species: Sordaria macrospora
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Sordaria; Sordaria macrospora
• CAZyme ID: SMAC_12587-t26_1-p1
• CAZy Family: GT69
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
427	NW_003546238|CGC8	45389.65	10.3911

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Smacrosporak-hell	11311	771870	484	10827

• Gene Location: location=NW_003546238:243562-244930(+)

Full Sequence      

MVTEKSHSTSAPGPKGTRKPKSYIESHSPSTYKQHHGGSLRSYIRGALGFLLILHGQTTS
VAAQSLNSTLVPTTLVSKAPIVSPASKPPPAVAPTSKPPLAVSHTSIPSSVPVPPSSTMK
GTSHPTSTPPNPTPIPIVITNSCPDTIWPGIGTQHGIGPGVGGFELAPGETRPLFVSPDW
QGRVWGRTNCSFNDEGTGPSNLNGVNGNGAACMTGDCFGRLDCEFTGQVPVTLAEFNLIG
GMNSDQTFYDISLVDGYNIPIGIIYIPAANTTWIPPNLTNCVCIASAGFLDPPSRSGFYY
TNKTFPMPGNRTKPTPPSAVGVPGTYKYTRPPNRETASIRTQTTQSNAPYSIRACRPVRR
RGTPKIAARASTTTPPCASRVCTARTQRQFVRTRTVMRLTIRPARSSFPMEAGGRWCFVQ
GAGARIF

Enzyme Prediction     

No EC number prediction in SMAC_12587-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	141	285	3.6e-35	0.5694444444444444

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185754	Thaumatin-like	7.04e-64	140	277	4	128	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.
395248	Thaumatin	3.62e-51	141	263	1	108	Thaumatin family.
185757	TLP-PA	1.67e-37	140	263	5	116	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	1.62e-29	141	263	5	115	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	1.27e-25	140	260	4	104	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
VBB73018.1|GH152	1.50e-94	131	339	117	324
UQC83697.1|GH152	1.55e-78	135	313	72	237
QBZ65635.1|GH152	1.29e-76	135	308	9	183
QPG96228.1|GH152	1.53e-73	135	308	56	216
QLI69933.1|GH152	3.19e-73	135	308	161	321

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4L2J_A	9.50e-19	134	261	1	108	Crystal Structure of Osmotin, an antifungal laticifer protein [Calotropis procera]
3ZS3_A	8.55e-18	137	263	3	118	High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
4JRU_A	3.19e-16	139	261	5	107	Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera]
1PCV_A	4.71e-16	137	261	3	108	Crystal structure of osmotin, a plant antifungal protein [Nicotiana tabacum],1PCV_B Crystal structure of osmotin, a plant antifungal protein [Nicotiana tabacum]
2AHN_A	4.78e-16	137	263	3	118	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P28493|PR5_ARATH	1.42e-26	139	263	28	137	Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1
sp|Q5DWG1|CRJ35_CRYJA	7.32e-26	139	263	27	136	Pathogenesis-related thaumatin-like protein 3.5 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|P32937|PR1A_HORVU	3.31e-23	139	259	25	125	Pathogenesis-related protein 1A/1B OS=Hordeum vulgare OX=4513 PE=2 SV=1
sp|P32938|PR1C_HORVU	1.20e-22	139	259	25	125	Pathogenesis-related protein 1C OS=Hordeum vulgare OX=4513 PE=2 SV=1
sp|A0A1P8B554|THLP1_ARATH	6.21e-22	137	261	35	154	Thaumatin-like protein 1 OS=Arabidopsis thaliana OX=3702 GN=TLP1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.959515	0.040481

TMHMM  Annotations     

There is no transmembrane helices in SMAC_12587-t26_1-p1.