Species | Albugo candida | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Oomycota; NA; ; Albuginaceae; Albugo; Albugo candida | |||||||||||
CAZyme ID | evm.model.AC2VRR_s00011g55-p1 | |||||||||||
CAZy Family | AA17 | |||||||||||
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 | 26 | 279 | 1.4e-56 | 0.9686274509803922 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
173825 | ascorbate_peroxidase | 9.00e-113 | 13 | 282 | 2 | 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 | 8.04e-65 | 43 | 278 | 32 | 243 | L-ascorbate peroxidase |
173823 | plant_peroxidase_like | 1.73e-57 | 26 | 276 | 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. |
178467 | PLN02879 | 3.01e-55 | 18 | 278 | 11 | 246 | L-ascorbate peroxidase |
166005 | PLN02364 | 1.62e-54 | 17 | 278 | 9 | 246 | L-ascorbate peroxidase 1 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
6.53e-99 | 16 | 283 | 62 | 331 | |
4.94e-78 | 14 | 283 | 78 | 350 | |
1.56e-74 | 18 | 283 | 106 | 366 | |
6.12e-71 | 27 | 283 | 12 | 274 | |
2.18e-69 | 38 | 282 | 110 | 349 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.53e-69 | 17 | 278 | 1 | 258 | Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major] |
|
2.61e-69 | 16 | 278 | 1 | 259 | The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin] |
|
2.61e-69 | 16 | 278 | 1 | 259 | 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] |
|
3.37e-69 | 17 | 278 | 1 | 258 | Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major] |
|
3.59e-69 | 17 | 278 | 1 | 258 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.12e-69 | 17 | 281 | 86 | 347 | 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 |
|
8.70e-69 | 13 | 283 | 78 | 348 | Cytochrome c peroxidase, mitochondrial OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=CCP1 PE=3 SV=1 |
|
1.31e-68 | 38 | 281 | 88 | 326 | Cytochrome c peroxidase, mitochondrial OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=CCP1 PE=3 SV=1 |
|
4.13e-68 | 25 | 279 | 7 | 261 | Putative cytochrome c peroxidase, mitochondrial OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=YALI0D04268g PE=3 SV=1 |
|
5.14e-68 | 38 | 279 | 175 | 413 | Putative heme-binding peroxidase OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=DEHA2G12166g PE=3 SV=3 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000060 | 0.000000 |
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