Species | Fusarium oxysporum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum | |||||||||||
CAZyme ID | FOMG_10186-t38_1-p1 | |||||||||||
CAZy Family | GH28 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA2 | 60 | 222 | 9.1e-27 | 0.6352941176470588 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
173829 | plant_peroxidase_like_1 | 3.89e-114 | 22 | 286 | 1 | 264 | 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. |
173823 | plant_peroxidase_like | 3.56e-21 | 64 | 285 | 19 | 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 | 4.27e-17 | 64 | 196 | 17 | 155 | Peroxidase. |
173825 | ascorbate_peroxidase | 9.05e-15 | 67 | 196 | 34 | 168 | Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water. |
173826 | ligninase | 2.33e-14 | 65 | 225 | 40 | 203 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 530 | 1 | 530 | |
0.0 | 1 | 530 | 1 | 530 | |
7.10e-105 | 16 | 519 | 15 | 521 | |
2.13e-99 | 7 | 489 | 7 | 488 | |
1.43e-96 | 7 | 489 | 7 | 488 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.21e-09 | 65 | 209 | 40 | 187 | 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] |
|
6.99e-09 | 65 | 209 | 40 | 187 | 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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3.91e-08 | 67 | 199 | 43 | 180 | Chain A, lignin peroxidase [Agrocybe pediades] |
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1.33e-07 | 67 | 196 | 47 | 181 | Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],1S6V_C Chain C, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],2N18_A Dominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidase [Saccharomyces cerevisiae S288C] |
|
1.33e-07 | 67 | 196 | 47 | 181 | K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex [Saccharomyces cerevisiae] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.02e-68 | 8 | 396 | 11 | 399 | WSC domain-containing protein ARB_07870 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07870 PE=1 SV=1 |
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2.79e-15 | 67 | 261 | 34 | 211 | L-ascorbate peroxidase 5, peroxisomal OS=Arabidopsis thaliana OX=3702 GN=APX5 PE=1 SV=2 |
|
5.93e-10 | 67 | 274 | 35 | 245 | L-ascorbate peroxidase 3 OS=Arabidopsis thaliana OX=3702 GN=APX3 PE=1 SV=1 |
|
3.41e-08 | 66 | 196 | 32 | 168 | Putative heme-binding peroxidase OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=AFUA_6G13570 PE=3 SV=1 |
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2.10e-07 | 67 | 196 | 96 | 230 | Cytochrome c peroxidase, mitochondrial OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=CCP1 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.984437 | 0.015593 |
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