Species | Colletotrichum graminicola | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Glomerellaceae; Colletotrichum; Colletotrichum graminicola | |||||||||||
CAZyme ID | EFQ25669.1 | |||||||||||
CAZy Family | AA2 | |||||||||||
CAZyme Description | Peroxidase [Source:UniProtKB/TrEMBL;Acc:E3Q3R7] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
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AA2 | 50 | 297 | 4.5e-53 | 0.9803921568627451 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
173826 | ligninase | 1.96e-64 | 46 | 309 | 16 | 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. |
173823 | plant_peroxidase_like | 3.03e-19 | 60 | 293 | 9 | 254 | Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase. |
395089 | peroxidase | 1.27e-16 | 50 | 204 | 1 | 150 | Peroxidase. |
173827 | secretory_peroxidase | 3.78e-12 | 43 | 293 | 11 | 279 | 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. |
173829 | plant_peroxidase_like_1 | 2.24e-08 | 73 | 186 | 46 | 151 | Uncharacterized family of plant peroxidase-like proteins. This is a subgroup of heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX) which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.56e-102 | 42 | 309 | 39 | 299 | |
2.61e-76 | 43 | 311 | 40 | 292 | |
7.07e-73 | 11 | 311 | 8 | 296 | |
3.38e-56 | 42 | 309 | 151 | 403 | |
4.57e-54 | 40 | 309 | 28 | 286 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
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9.19e-27 | 59 | 306 | 28 | 279 | 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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4.60e-26 | 62 | 306 | 38 | 293 | Chain A, Ligninase H8 [Phanerochaete chrysosporium RP-78],6ISS_G Chain G, Ligninase H8 [Phanerochaete chrysosporium RP-78] |
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1.11e-25 | 62 | 306 | 32 | 287 | Chain A, Lignin Peroxidase [Phanerodontia chrysosporium],1QPA_B Chain B, Lignin Peroxidase [Phanerodontia chrysosporium] |
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6.29e-25 | 59 | 306 | 28 | 279 | 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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1.85e-24 | 59 | 306 | 28 | 279 | 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 |
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6.04e-25 | 62 | 306 | 60 | 315 | Ligninase H2 OS=Phanerodontia chrysosporium OX=2822231 GN=GLG4 PE=1 SV=2 |
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4.73e-23 | 59 | 306 | 52 | 310 | Manganese peroxidase 3 OS=Phlebia radiata OX=5308 GN=mnp3 PE=2 SV=1 |
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6.43e-23 | 59 | 306 | 58 | 309 | Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1 |
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1.22e-22 | 59 | 306 | 58 | 309 | Versatile peroxidase VPL2 OS=Pleurotus eryngii OX=5323 GN=vpl2 PE=1 SV=1 |
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2.62e-22 | 62 | 306 | 59 | 314 | Ligninase H8 OS=Phanerodontia chrysosporium OX=2822231 GN=LPOA PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000260 | 0.999700 | CS pos: 20-21. Pr: 0.9487 |
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