Species | Phytophthora ramorum | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora ramorum | |||||||||||
CAZyme ID | PSURA_38638T0-p1 | |||||||||||
CAZy Family | AA1 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA2 | 11 | 262 | 1.6e-58 | 0.9490196078431372 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
173825 | ascorbate_peroxidase | 9.17e-134 | 1 | 264 | 9 | 251 | 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 | 1.65e-73 | 24 | 264 | 32 | 245 | L-ascorbate peroxidase |
166005 | PLN02364 | 1.42e-58 | 23 | 262 | 33 | 246 | L-ascorbate peroxidase 1 |
178467 | PLN02879 | 1.73e-57 | 19 | 262 | 30 | 246 | L-ascorbate peroxidase |
173823 | plant_peroxidase_like | 1.81e-56 | 7 | 260 | 2 | 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 |
---|---|---|---|---|---|
1.66e-168 | 1 | 264 | 66 | 328 | |
1.18e-90 | 4 | 264 | 107 | 363 | |
2.27e-89 | 13 | 263 | 95 | 336 | |
5.53e-88 | 8 | 263 | 99 | 346 | |
1.00e-87 | 16 | 263 | 112 | 350 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.48e-76 | 2 | 264 | 5 | 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] |
|
1.97e-76 | 2 | 264 | 5 | 260 | Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major] |
|
2.10e-76 | 2 | 264 | 5 | 260 | Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major] |
|
2.17e-76 | 2 | 264 | 6 | 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] |
|
7.04e-75 | 2 | 264 | 6 | 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 |
---|---|---|---|---|---|---|
1.02e-90 | 16 | 263 | 112 | 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 |
|
7.73e-86 | 4 | 263 | 86 | 342 | 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 |
|
1.25e-84 | 4 | 263 | 90 | 339 | 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 |
|
2.05e-84 | 16 | 263 | 130 | 368 | Cytochrome c peroxidase, mitochondrial OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP1 PE=3 SV=1 |
|
3.87e-84 | 7 | 263 | 96 | 345 | Cytochrome c peroxidase, mitochondrial OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=ccp1 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000066 | 0.000002 |
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