Species | Coprinopsis cinerea | |||||||||||
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Lineage | Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea | |||||||||||
CAZyme ID | CC1G_00690-t26_1-p1 | |||||||||||
CAZy Family | AA1 | |||||||||||
CAZyme Description | laccase 5 | |||||||||||
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 | 41 | 341 | 5.8e-142 | 0.9834983498349835 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
259925 | CuRO_1_Tv-LCC_like | 6.94e-73 | 30 | 153 | 3 | 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. |
274555 | ascorbase | 2.42e-67 | 34 | 493 | 8 | 530 | 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. |
274556 | laccase | 2.50e-66 | 45 | 500 | 21 | 534 | laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate. |
259949 | CuRO_2_Tv-LCC_like | 5.10e-66 | 169 | 320 | 1 | 154 | 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. |
259970 | CuRO_3_Tv-LCC_like | 4.71e-64 | 348 | 488 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 526 | 1 | 533 | |
0.0 | 1 | 526 | 1 | 533 | |
3.01e-251 | 8 | 524 | 8 | 525 | |
7.50e-242 | 31 | 526 | 32 | 533 | |
2.43e-201 | 26 | 525 | 32 | 552 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.67e-190 | 24 | 521 | 1 | 503 | Chain A, LACCASE 1 [Coprinopsis cinerea] |
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2.45e-190 | 25 | 521 | 2 | 503 | Chain A, Laccase [Coprinopsis cinerea] |
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2.27e-176 | 26 | 514 | 2 | 494 | T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata] |
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1.77e-175 | 26 | 511 | 2 | 490 | 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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6.87e-173 | 26 | 513 | 2 | 493 | PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.99e-178 | 11 | 511 | 8 | 515 | Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1 |
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5.31e-175 | 11 | 514 | 8 | 518 | Laccase-1 OS=Trametes villosa OX=47662 GN=LCC1 PE=1 SV=1 |
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2.10e-169 | 26 | 511 | 24 | 515 | Laccase-4 OS=Trametes versicolor OX=5325 GN=LCC4 PE=3 SV=1 |
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5.97e-169 | 26 | 511 | 24 | 515 | Laccase-4 OS=Trametes villosa OX=47662 GN=LCC4 PE=3 SV=1 |
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7.90e-169 | 11 | 514 | 8 | 516 | Laccase OS=Pycnoporus cinnabarinus OX=5643 GN=LCC3-1 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000488 | 0.999486 | CS pos: 22-23. Pr: 0.9737 |
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