Species | Hemileia vastatrix | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Basidiomycota; Pucciniomycetes; ; Zaghouaniaceae; Hemileia; Hemileia vastatrix | |||||||||||
CAZyme ID | HVAS_10124010.1-p1 | |||||||||||
CAZy Family | GH26 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA2 | 41 | 187 | 8.5e-39 | 0.5607843137254902 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
173825 | ascorbate_peroxidase | 4.61e-72 | 21 | 185 | 12 | 172 | 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 | 5.36e-44 | 42 | 188 | 32 | 173 | L-ascorbate peroxidase |
178467 | PLN02879 | 9.15e-42 | 22 | 185 | 6 | 173 | L-ascorbate peroxidase |
166005 | PLN02364 | 1.17e-37 | 42 | 185 | 34 | 173 | L-ascorbate peroxidase 1 |
395089 | peroxidase | 9.70e-35 | 25 | 182 | 1 | 156 | Peroxidase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
4.88e-54 | 21 | 188 | 90 | 259 | |
1.25e-53 | 14 | 188 | 150 | 326 | |
1.14e-52 | 21 | 188 | 90 | 259 | |
1.14e-52 | 21 | 188 | 90 | 259 | |
1.14e-52 | 21 | 188 | 90 | 259 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.54e-42 | 21 | 185 | 18 | 178 | Chain A, Cytochrome c peroxidase [synthetic construct] |
|
2.70e-42 | 21 | 185 | 20 | 187 | cytochrome c peroxidase M119W in complex with guiacol [Saccharomyces cerevisiae] |
|
4.99e-42 | 21 | 185 | 17 | 184 | Joint Neutron and X-ray structure of Cytochrome c peroxidase [Saccharomyces cerevisiae],3R99_A Joint Neutron and X-ray structure of Cytochrome c peroxidase [Saccharomyces cerevisiae],4XVA_A Crystal structure of wild type cytochrome c peroxidase [Saccharomyces cerevisiae S288C],4XVA_C Crystal structure of wild type cytochrome c peroxidase [Saccharomyces cerevisiae S288C],4XVA_E Crystal structure of wild type cytochrome c peroxidase [Saccharomyces cerevisiae S288C],4XVA_G Crystal structure of wild type cytochrome c peroxidase [Saccharomyces cerevisiae S288C] |
|
5.11e-42 | 21 | 185 | 18 | 185 | Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP) [Saccharomyces cerevisiae],1S73_A Crystal Structure of Mesopone Cytochrome c Peroxidase (R-isomer) [MpCcP-R] [Saccharomyces cerevisiae],1SBM_A Crystal Structure of Reduced Mesopone cytochrome c peroxidase (R-isomer) [Saccharomyces cerevisiae],1SDQ_A Structure of reduced-NO adduct of mesopone cytochrome c peroxidase [Saccharomyces cerevisiae],1Z53_A The 1.13 Angstrom Structure of Iron-free Cytochrome c Peroxidase [Saccharomyces cerevisiae],1ZBY_A High-Resolution Crystal Structure of Native (Resting) Cytochrome c Peroxidase (CcP) [Saccharomyces cerevisiae],1ZBZ_A High-Resolution Crystal Structure of Compound I intermediate of Cytochrome c Peroxidase (CcP) [Saccharomyces cerevisiae],2B0Z_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],2B10_A Crystal Structure of the Protein-Protein Complex between F82S cytochrome c and cytochrome c peroxidase [Saccharomyces cerevisiae],2B10_C Crystal Structure of the Protein-Protein Complex between F82S cytochrome c and cytochrome c peroxidase [Saccharomyces cerevisiae],2B11_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],2B11_C Chain C, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],2B12_A Chain A, Cytochrome c peroxidase, mitochondrial [Saccharomyces cerevisiae],2CYP_A Crystal structure of yeast cytochrome C peroxidase refined at 1.7-angstroms resolution [Saccharomyces cerevisiae],2YCG_A Structure of unreduced ferric cytochrome c peroxidase obtained by multicrystal method [Saccharomyces cerevisiae] |
|
5.11e-42 | 21 | 185 | 18 | 185 | Chain A, Cytochrome c Peroxidase [Saccharomyces cerevisiae] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.91e-52 | 21 | 188 | 94 | 263 | Cytochrome c peroxidase, mitochondrial OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=ccp1 PE=3 SV=1 |
|
7.37e-52 | 21 | 188 | 112 | 281 | Cytochrome c peroxidase, mitochondrial OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP1 PE=3 SV=1 |
|
1.72e-51 | 21 | 188 | 89 | 258 | 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 |
|
2.16e-50 | 21 | 185 | 5 | 171 | Putative cytochrome c peroxidase, mitochondrial OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=YALI0D04268g PE=3 SV=1 |
|
3.20e-50 | 21 | 185 | 68 | 234 | 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 |
---|---|---|
1.000074 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.