Species | Allomyces macrogynus | |||||||||||
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Lineage | Blastocladiomycota; Blastocladiomycetes; ; Blastocladiaceae; Allomyces; Allomyces macrogynus | |||||||||||
CAZyme ID | AMAG_11933-t26_1-p1 | |||||||||||
CAZy Family | GT2 | |||||||||||
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 | 1 | 161 | 1e-34 | 0.611764705882353 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
173825 | ascorbate_peroxidase | 3.04e-80 | 1 | 164 | 105 | 253 | 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. |
178218 | PLN02608 | 6.08e-54 | 2 | 162 | 107 | 245 | L-ascorbate peroxidase |
178467 | PLN02879 | 9.62e-45 | 2 | 160 | 110 | 246 | L-ascorbate peroxidase |
166005 | PLN02364 | 4.99e-44 | 2 | 160 | 109 | 246 | L-ascorbate peroxidase 1 |
173823 | plant_peroxidase_like | 1.20e-35 | 1 | 158 | 99 | 255 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
7.95e-69 | 1 | 163 | 105 | 270 | |
8.18e-69 | 1 | 163 | 105 | 270 | |
3.91e-68 | 1 | 163 | 117 | 281 | |
3.91e-68 | 1 | 163 | 117 | 281 | |
3.91e-68 | 1 | 163 | 117 | 281 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.93e-47 | 1 | 162 | 102 | 260 | Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major] |
|
5.27e-47 | 1 | 162 | 102 | 260 | Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major] |
|
5.56e-47 | 1 | 162 | 102 | 260 | Structure of Leishmania major peroxidase D211R mutant (high res) [Leishmania major],5ALA_A Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major],5ALA_B Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major] |
|
5.71e-47 | 1 | 162 | 103 | 261 | The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin] |
|
1.81e-45 | 1 | 162 | 103 | 261 | The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin],3RIW_B The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.84e-68 | 1 | 163 | 105 | 270 | Putative heme-binding peroxidase OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP2 PE=3 SV=1 |
|
1.02e-65 | 1 | 163 | 117 | 281 | Putative heme-binding peroxidase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FGRRES_10606 PE=3 SV=1 |
|
1.08e-65 | 1 | 163 | 104 | 263 | Putative cytochrome c peroxidase, mitochondrial OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=YALI0D04268g PE=3 SV=1 |
|
2.15e-64 | 1 | 161 | 194 | 350 | Cytochrome c peroxidase, mitochondrial OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=ccp1 PE=3 SV=1 |
|
2.72e-64 | 1 | 163 | 105 | 271 | Putative heme-binding peroxidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=AN5440 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000038 | 0.000000 |
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