Species | Phytophthora parasitica | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica | |||||||||||
CAZyme ID | PPTG_08286-t26_1-p1 | |||||||||||
CAZy Family | GH17 | |||||||||||
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 | 69 | 322 | 7e-59 | 0.9607843137254902 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
173825 | ascorbate_peroxidase | 4.21e-149 | 57 | 326 | 4 | 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 | 9.72e-81 | 85 | 329 | 32 | 250 | L-ascorbate peroxidase |
166005 | PLN02364 | 4.57e-63 | 84 | 322 | 33 | 246 | L-ascorbate peroxidase 1 |
178467 | PLN02879 | 2.99e-62 | 80 | 322 | 30 | 246 | L-ascorbate peroxidase |
173823 | plant_peroxidase_like | 5.00e-61 | 67 | 320 | 1 | 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 |
---|---|---|---|---|---|
1.01e-202 | 1 | 334 | 1 | 339 | |
8.36e-91 | 58 | 327 | 79 | 340 | |
1.26e-90 | 67 | 325 | 97 | 348 | |
1.42e-90 | 62 | 327 | 92 | 366 | |
4.72e-87 | 67 | 336 | 100 | 363 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.64e-79 | 59 | 324 | 1 | 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] |
|
8.92e-79 | 58 | 324 | 1 | 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] |
|
1.15e-78 | 59 | 324 | 1 | 260 | Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major] |
|
1.22e-78 | 59 | 324 | 1 | 260 | Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major] |
|
2.87e-77 | 58 | 324 | 1 | 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 |
---|---|---|---|---|---|---|
1.73e-90 | 67 | 325 | 100 | 352 | Cytochrome c peroxidase, mitochondrial OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=ccp1 PE=3 SV=1 |
|
1.32e-86 | 77 | 323 | 130 | 368 | Cytochrome c peroxidase, mitochondrial OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP1 PE=3 SV=1 |
|
2.24e-86 | 65 | 328 | 86 | 347 | Cytochrome c peroxidase, mitochondrial OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=ccp-1 PE=3 SV=1 |
|
7.17e-85 | 68 | 327 | 92 | 343 | Cytochrome c peroxidase, mitochondrial OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=CCP1 PE=3 SV=1 |
|
4.58e-84 | 77 | 327 | 106 | 348 | Cytochrome c peroxidase, mitochondrial OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=CCP1 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.999907 | 0.000131 |
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