Species | Coprinopsis cinerea | |||||||||||
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Lineage | Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea | |||||||||||
CAZyme ID | CC1G_02533-t26_1-p1 | |||||||||||
CAZy Family | AA7 | |||||||||||
CAZyme Description | laccase 3 | |||||||||||
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 | 31 | 335 | 8.4e-155 | 0.9933993399339934 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
259970 | CuRO_3_Tv-LCC_like | 2.17e-82 | 343 | 489 | 1 | 147 | The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. 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. 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. |
259949 | CuRO_2_Tv-LCC_like | 2.07e-81 | 165 | 315 | 1 | 157 | The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. 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. Laccase is a multicopper oxidase (MCO) composed of three cupredoxin domains 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 2 of 3-domain MCOs has lost the ability to bind copper. |
274555 | ascorbase | 8.91e-77 | 32 | 489 | 14 | 525 | 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. |
259925 | CuRO_1_Tv-LCC_like | 1.15e-70 | 20 | 149 | 1 | 125 | The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. 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. 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. |
177843 | PLN02191 | 9.90e-70 | 51 | 492 | 50 | 551 | L-ascorbate oxidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 516 | 1 | 516 | |
0.0 | 1 | 516 | 1 | 516 | |
0.0 | 1 | 516 | 1 | 516 | |
1.08e-312 | 12 | 516 | 14 | 518 | |
7.37e-306 | 1 | 515 | 1 | 517 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.22e-229 | 17 | 516 | 1 | 495 | Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena] |
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4.04e-229 | 17 | 511 | 1 | 494 | Chain A, LACCASE 2 [Trametes versicolor] |
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5.31e-227 | 2 | 513 | 6 | 515 | Crystal structure of laccases from Pycnoporus sanguineus, izoform II [Trametes coccinea],5NQ9_A Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea],5NQ9_C Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea] |
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7.67e-227 | 17 | 516 | 1 | 499 | Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta] |
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1.54e-226 | 17 | 516 | 1 | 499 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.41e-243 | 14 | 511 | 21 | 522 | Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1 |
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1.74e-239 | 15 | 511 | 22 | 520 | Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1 |
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1.83e-229 | 16 | 511 | 20 | 514 | Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1 |
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3.81e-229 | 2 | 511 | 6 | 515 | Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1 |
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2.19e-228 | 14 | 511 | 19 | 515 | Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2 |
Other | SP_Sec_SPI | CS Position |
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0.000327 | 0.999665 | CS pos: 16-17. Pr: 0.9782 |
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