Species | Botrytis cinerea | |||||||||||
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Lineage | Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Botrytis; Botrytis cinerea | |||||||||||
CAZyme ID | Bcin13g03680.1:RNA-p1 | |||||||||||
CAZy Family | GT1 | |||||||||||
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 | 61 | 243 | 5.6e-24 | 0.6941176470588235 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
173829 | plant_peroxidase_like_1 | 1.83e-136 | 23 | 285 | 1 | 264 | Uncharacterized family of plant peroxidase-like proteins. This is a subgroup of 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. |
173823 | plant_peroxidase_like | 3.45e-24 | 55 | 284 | 9 | 254 | 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. |
395089 | peroxidase | 2.77e-17 | 61 | 197 | 13 | 155 | Peroxidase. |
173825 | ascorbate_peroxidase | 7.80e-15 | 68 | 239 | 34 | 201 | 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. |
173826 | ligninase | 2.88e-10 | 64 | 239 | 38 | 214 | Ligninase and other manganese-dependent fungal peroxidases. Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.23e-121 | 1 | 533 | 1 | 529 | |
3.88e-120 | 1 | 533 | 1 | 529 | |
4.41e-114 | 14 | 536 | 13 | 535 | |
6.81e-114 | 7 | 536 | 5 | 538 | |
1.38e-112 | 14 | 536 | 13 | 535 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.99e-06 | 68 | 232 | 30 | 191 | Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major] |
|
5.02e-06 | 68 | 232 | 31 | 192 | 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] |
|
6.58e-06 | 68 | 232 | 30 | 191 | Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major] |
|
6.67e-06 | 68 | 232 | 30 | 191 | 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] |
|
6.71e-06 | 68 | 232 | 31 | 192 | The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.05e-91 | 17 | 536 | 17 | 515 | WSC domain-containing protein ARB_07870 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07870 PE=1 SV=1 |
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8.54e-10 | 64 | 194 | 114 | 247 | Putative L-ascorbate peroxidase 6 OS=Arabidopsis thaliana OX=3702 GN=APX6 PE=2 SV=1 |
|
2.10e-08 | 68 | 220 | 35 | 187 | Probable L-ascorbate peroxidase 4, peroxisomal OS=Oryza sativa subsp. japonica OX=39947 GN=APX4 PE=2 SV=1 |
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3.46e-08 | 63 | 296 | 50 | 313 | Peroxidase 70 OS=Zea mays OX=4577 GN=PER70 PE=1 SV=1 |
|
4.25e-08 | 68 | 197 | 117 | 251 | 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 |
---|---|---|
0.000374 | 0.999582 | CS pos: 19-20. Pr: 0.9764 |
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