Species | Hemileia vastatrix | |||||||||||
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Lineage | Basidiomycota; Pucciniomycetes; ; Zaghouaniaceae; Hemileia; Hemileia vastatrix | |||||||||||
CAZyme ID | HVAS_10079770.1-p1 | |||||||||||
CAZy Family | GH18 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 1.10.3.2:77 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA1 | 53 | 417 | 3.6e-102 | 0.9776536312849162 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
259926 | CuRO_1_Diphenol_Ox | 6.89e-68 | 37 | 156 | 1 | 119 | The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. |
274555 | ascorbase | 1.69e-57 | 36 | 436 | 1 | 536 | L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases. |
259923 | CuRO_1_MaLCC_like | 2.22e-51 | 35 | 156 | 2 | 122 | The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. |
215324 | PLN02604 | 7.91e-50 | 35 | 335 | 23 | 323 | oxidoreductase |
177843 | PLN02191 | 2.87e-49 | 37 | 436 | 24 | 559 | L-ascorbate oxidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.07e-99 | 33 | 439 | 95 | 604 | |
4.60e-98 | 7 | 442 | 85 | 621 | |
5.75e-88 | 29 | 436 | 90 | 610 | |
2.41e-70 | 19 | 439 | 105 | 655 | |
2.46e-68 | 34 | 375 | 121 | 471 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.39e-51 | 38 | 433 | 5 | 479 | Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta] |
|
2.39e-51 | 38 | 433 | 5 | 479 | Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta] |
|
6.98e-50 | 49 | 422 | 17 | 467 | Chain A, LACCASE 1 [Coprinopsis cinerea] |
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7.11e-50 | 49 | 422 | 17 | 467 | Chain A, Laccase [Coprinopsis cinerea] |
|
2.42e-49 | 38 | 433 | 5 | 479 | Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.53e-54 | 16 | 441 | 1 | 511 | Laccase-2 OS=Agaricus bisporus OX=5341 GN=lcc2 PE=1 SV=1 |
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6.53e-54 | 16 | 441 | 1 | 511 | Laccase-1 OS=Agaricus bisporus OX=5341 GN=lcc1 PE=1 SV=1 |
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8.27e-51 | 37 | 399 | 23 | 377 | Laccase-4 OS=Thanatephorus cucumeris OX=107832 GN=LCC4 PE=1 SV=1 |
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9.63e-51 | 15 | 451 | 1 | 526 | Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1 |
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4.71e-49 | 36 | 451 | 24 | 527 | Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000028 | 0.000000 |
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