Species | Coprinopsis cinerea | |||||||||||
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Lineage | Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea | |||||||||||
CAZyme ID | CC1G_05965-t26_1-p1 | |||||||||||
CAZy Family | GH11 | |||||||||||
CAZyme Description | laccase 8 | |||||||||||
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 | 191 | 493 | 9.8e-146 | 0.9900990099009901 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
274555 | ascorbase | 1.08e-88 | 191 | 646 | 14 | 523 | 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. |
259970 | CuRO_3_Tv-LCC_like | 3.54e-78 | 501 | 648 | 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. |
259925 | CuRO_1_Tv-LCC_like | 8.12e-77 | 179 | 303 | 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 | 1.05e-74 | 191 | 646 | 36 | 546 | L-ascorbate oxidase |
215324 | PLN02604 | 4.07e-74 | 191 | 646 | 37 | 546 | oxidoreductase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 165 | 728 | 4 | 567 | |
0.0 | 165 | 728 | 4 | 567 | |
8.08e-237 | 172 | 680 | 15 | 532 | |
9.30e-236 | 177 | 680 | 28 | 532 | |
9.96e-231 | 182 | 681 | 32 | 532 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.03e-223 | 177 | 674 | 2 | 496 | Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus] |
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8.75e-222 | 177 | 681 | 3 | 503 | Chain A, LACCASE 1 [Coprinopsis cinerea] |
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9.07e-222 | 177 | 681 | 3 | 503 | Chain A, Laccase [Coprinopsis cinerea] |
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5.51e-221 | 177 | 673 | 2 | 493 | Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii] |
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6.84e-221 | 177 | 674 | 2 | 500 | Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.21e-218 | 177 | 674 | 23 | 518 | Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2 |
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5.36e-216 | 177 | 674 | 23 | 516 | Laccase OS=Pycnoporus cinnabarinus OX=5643 GN=LCC3-1 PE=1 SV=1 |
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9.35e-215 | 177 | 674 | 23 | 518 | Laccase-1 OS=Trametes villosa OX=47662 GN=LCC1 PE=1 SV=1 |
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5.15e-214 | 177 | 671 | 22 | 514 | Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1 |
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7.56e-214 | 177 | 674 | 24 | 518 | Laccase-4 OS=Trametes versicolor OX=5325 GN=LCC4 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.048533 | 0.951445 | CS pos: 23-24. Pr: 0.8475 |
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