Species | Magnaporthiopsis poae | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae | |||||||||||
CAZyme ID | KLU90766.1 | |||||||||||
CAZy Family | GH74 | |||||||||||
CAZyme Description | Peroxidase [Source:UniProtKB/TrEMBL;Acc:A0A0C4ED24] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA2 | 1 | 158 | 1.9e-33 | 0.6588235294117647 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
173826 | ligninase | 2.70e-58 | 2 | 170 | 108 | 287 | Ligninase and other manganese-dependent fungal peroxidases. Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites. |
173827 | secretory_peroxidase | 1.29e-17 | 2 | 153 | 100 | 278 | Horseradish peroxidase and related secretory plant peroxidases. Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites. |
395089 | peroxidase | 3.93e-13 | 1 | 69 | 80 | 150 | Peroxidase. |
166005 | PLN02364 | 7.04e-07 | 15 | 107 | 109 | 201 | L-ascorbate peroxidase 1 |
178218 | PLN02608 | 9.22e-06 | 15 | 69 | 107 | 161 | L-ascorbate peroxidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.68e-81 | 1 | 171 | 132 | 300 | |
7.01e-64 | 1 | 170 | 127 | 290 | |
1.76e-55 | 1 | 170 | 126 | 294 | |
3.56e-40 | 4 | 170 | 169 | 340 | |
1.70e-37 | 1 | 170 | 180 | 348 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.46e-24 | 2 | 170 | 103 | 282 | Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37k, H39r, V160a, T184m, Q202l, D213a & G330r [Pleurotus eryngii],5FNB_B Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37k, H39r, V160a, T184m, Q202l, D213a & G330r [Pleurotus eryngii] |
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8.99e-24 | 2 | 170 | 103 | 282 | CRYSTAL STRUCTURE ANALYSIS OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII. MUTANT VPi-SS. MUTATED RESIDUES T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K AND A314R. [Pleurotus eryngii] |
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8.99e-24 | 2 | 170 | 103 | 282 | CRYSTAL STRUCTURE ANALYSIS OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII. MUTANT VPi-br. MUTATED RESIDUES T2K, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R, A309K AND A314R. [Pleurotus eryngii] |
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9.11e-24 | 2 | 170 | 104 | 283 | CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM I [Pleurotus ostreatus],4BLL_A CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM II [Pleurotus ostreatus],4BLN_A CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM III [Pleurotus ostreatus],4BLX_A CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM IV [Pleurotus ostreatus],4BLY_A Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form V [Pleurotus ostreatus],4BLZ_A Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form Vi [Pleurotus ostreatus],4BLZ_B Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form Vi [Pleurotus ostreatus],4BM0_A Crystal Structure Of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form Vii [Pleurotus ostreatus] |
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1.44e-23 | 2 | 170 | 103 | 282 | Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus eryngii Versatile Peroxidase [Pleurotus eryngii] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.81e-23 | 2 | 170 | 133 | 313 | Manganese peroxidase 3 OS=Phlebia radiata OX=5308 GN=mnp3 PE=2 SV=1 |
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4.56e-23 | 1 | 167 | 111 | 286 | Low-redox potential peroxidase OS=Taiwanofungus camphoratus OX=2696576 GN=LnP PE=1 SV=1 |
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6.57e-22 | 2 | 170 | 133 | 312 | Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1 |
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9.11e-22 | 2 | 170 | 133 | 312 | Versatile peroxidase VPL2 OS=Pleurotus eryngii OX=5323 GN=vpl2 PE=1 SV=1 |
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2.31e-18 | 2 | 170 | 140 | 319 | Versatile peroxidase VPS1 OS=Pleurotus eryngii OX=5323 GN=vps1 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.999959 | 0.000069 |
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