CAZyme Information: AGR57_8385T0-p1

Basic Information

• Species: Phanerochaete chrysosporium
• Lineage: Basidiomycota; Agaricomycetes; ; Phanerochaetaceae; Phanerochaete; Phanerochaete chrysosporium
• CAZyme ID: AGR57_8385T0-p1
• CAZy Family: GT2
• CAZyme Description: thaumatin-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
255	PchrRP-78_SC008|CGC2	26779.73	4.8925

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PchrysosporiumRP-78	13602	273507	0	13602

• Gene Location: location=PchrRP-78_SC008:680867-682131(+)

Full Sequence      

MKLTSTLYAASLVAVCSARTFTVHNGCSFTIWPAIFTDLNVGSAKPDFATGWQADPHTSV
NFTVPDNWKSGRIWGRRDCDFSDPNPATQCADGGCNGGLLCDPHSGTGVPPATLAEFTLG
GGQDNYDVSIVDGFNLPMRIDNNKGCGVPSCPVDLIPHCPKPLKGPLNSAGSPVGCRSAC
NANLDGHPTNSSNCCSGQYSTPETCPSSGVAYYSYFKGNCPNSYAYAYDESSGTALFTCD
SALAADYTITFCPSK

Enzyme Prediction     

EC	3.2.1.39:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	25	253	1.7e-70	0.9953703703703703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185758	TLP-F	4.28e-103	21	253	1	229	thaumatin-like proteins: basidiomycete homologs. This subfamily is represented by Lentinula edodes TLG1, a thaumatin-like protein (TLP), as well as, other basidiomycete homologs. In general, TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. TLG1 TLP is involved in lentinan degradation and fruiting body senescence. TLG1 expressed in Escherichia coli and Aspergillus oryzae exhibited beta-1,3-glucanase activity and demonstrated lentinan degrading activity. TLG1 is proposed to be involved in lentinan and cell wall degradation during senescence following harvest and spore diffusion. TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. TLG1 from Lentinula edodes contains the required acidic amino acids conserved in the appropriate positions to possess an electronegative cleft. TLPs within this subfamily contain 13 conserved Cys residues; the number of total Cys residues in these TLPs varies from 16 in L. edodes TLG1 to 18 in other basidiomycete homologs.
395248	Thaumatin	1.81e-91	25	253	1	211	Thaumatin family.
185757	TLP-PA	1.73e-69	20	252	1	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	1.43e-53	21	253	1	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.
185754	Thaumatin-like	5.38e-44	21	252	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANC28050.1|GH152	3.98e-135	9	253	6	254
QRW11201.1|GH152	5.73e-127	10	253	7	252
QRV82455.1|GH152	5.73e-127	10	253	7	252
QRW10367.1|GH152	2.19e-125	2	253	3	256
QRV81581.1|GH152	2.19e-125	2	253	3	256

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZS3_A	1.10e-42	22	253	4	222	High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
2AHN_A	4.85e-41	20	253	2	222	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
4L5H_A	1.98e-33	20	253	2	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]
6E0D_A	1.27e-29	12	254	16	228	X-ray structure of a complex of thaumatin with xylene cyanol [Thaumatococcus daniellii]
1RQW_A	6.89e-29	20	254	2	206	Thaumatin Structure at 1.05 A Resolution [Thaumatococcus daniellii],1THU_A The Structures Of Three Crystal Forms Of The Sweet Protein Thaumatin [Thaumatococcus daniellii],1THW_A The Structures Of Three Crystal Forms Of The Sweet Protein Thaumatin [Thaumatococcus daniellii],2A7I_X On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength [Thaumatococcus daniellii],2G4Y_A structure of thaumatin at 2.0 A wavelength [Thaumatococcus daniellii],3DZN_A Thaumatin by LB nanotemplate method before high X-Ray dose on ESRF ID29 beamline [Thaumatococcus daniellii],3DZP_A Thaumatin by LB nanotemplate method after high X-Ray dose on ESRF ID29 beamline [Thaumatococcus daniellii],3DZR_A Thaumatin by Classical hanging drop method before high X-Ray dose on ESRF ID29 beamline [Thaumatococcus daniellii],3E0A_A Thaumatin by Classical hanging drop method after high X-Ray dose on ESRF ID29 beamline [Thaumatococcus daniellii],4DIY_A Thaumatin I by Classical Hanging Drop Method at 1.98A resolution for Unique Water Distribution [Thaumatococcus daniellii],4DIZ_A Thaumatin I by Classical Hanging Drop Method at 1.98A resolution for Unique Water Distribution [Thaumatococcus daniellii],4DJ0_A Thaumatin I by Langmuir-Blodgett Hanging Drop Method at 1.98A resolution for Unique Water Distribution [Thaumatococcus daniellii],4DJ1_A Thaumatin I by Langmuir-Blodgett Hanging Drop Method at 1.98A resolution for Unique Water Distribution [Thaumatococcus daniellii],4EK0_A Initial Thaumatin Structure for Radiation Damage Experiment at 25 K [Thaumatococcus daniellii],4EKA_A Final Thaumatin Structure for Radiation Damage Experiment at 25 K [Thaumatococcus daniellii],4EKB_A Initial Thaumatin Structure for Radiation Damage Experiment at 100 K [Thaumatococcus daniellii],4EKH_A Final Thaumatin Structure for Radiation Damage Experiment at 100 K [Thaumatococcus daniellii],4EKO_A Initial Thaumatin Structure for Radiation Damage Experiment at 180 K [Thaumatococcus daniellii],4EKT_A Final Thaumatin Structure for Radiation Damage Experiment at 180 K [Thaumatococcus daniellii],4EL2_A Initial Thaumatin Structure for Radiation Damage Experiment at 240 K [Thaumatococcus daniellii],4EL3_A Final Thaumatin Structure for Radiation Damage Experiment at 240 K [Thaumatococcus daniellii],4EL7_A Initial Thaumatin Structure for Radiation Damage Experiment at 300 K [Thaumatococcus daniellii],4ELA_A Final Thaumatin Structure for Radiation Damage Experiment at 300 K [Thaumatococcus daniellii],6C6W_A Structure of a Complex Between Thaumatin and Thioflavin T [Thaumatococcus daniellii],7LFG_A Chain A, Thaumatin I [Thaumatococcus daniellii],7LJV_A Chain A, Thaumatin I [Thaumatococcus daniellii],7LJW_A Chain A, Thaumatin I [Thaumatococcus daniellii],7LJZ_A Chain A, Thaumatin I [Thaumatococcus daniellii],7LK5_A Chain A, Thaumatin I [Thaumatococcus daniellii],7LK6_A Chain A, Thaumatin I [Thaumatococcus daniellii],7LNB_A Chain A, Thaumatin I [Thaumatococcus daniellii],7LNC_A Chain A, Thaumatin I [Thaumatococcus daniellii],7LND_A Chain A, Thaumatin I [Thaumatococcus daniellii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1P8B554|THLP1_ARATH	5.30e-46	20	254	34	257	Thaumatin-like protein 1 OS=Arabidopsis thaliana OX=3702 GN=TLP1 PE=2 SV=1
sp|Q5DWG1|CRJ35_CRYJA	9.55e-45	18	255	22	240	Pathogenesis-related thaumatin-like protein 3.5 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|O80327|TLP1_PYRPY	1.32e-42	7	253	12	244	Thaumatin-like protein 1 OS=Pyrus pyrifolia OX=3767 GN=TL1 PE=1 SV=1
sp|Q9FSG7|TP1A_MALDO	5.51e-42	18	253	24	246	Thaumatin-like protein 1a OS=Malus domestica OX=3750 GN=TL1 PE=1 SV=1
sp|P50694|TLP_PRUAV	1.18e-40	18	253	23	245	Glucan endo-1,3-beta-glucosidase OS=Prunus avium OX=42229 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000216	0.999725	CS pos: 18-19. Pr: 0.9681

TMHMM  Annotations     

There is no transmembrane helices in AGR57_8385T0-p1.