Species | Aspergillus oryzae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae | |||||||||||
CAZyme ID | AO090011000755-T-p1 | |||||||||||
CAZy Family | GH18 | |||||||||||
CAZyme Description | Putative multicopper oxidase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA1 | 38 | 590 | 7.1e-77 | 0.9804469273743017 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
259965 | CuRO_3_Abr2_like | 3.28e-69 | 425 | 596 | 1 | 164 | The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), laccase is 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 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. |
259944 | CuRO_2_Abr2_like | 1.73e-57 | 171 | 369 | 3 | 138 | The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), laccase is 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. |
259919 | CuRO_1_Abr2_like | 5.11e-52 | 25 | 139 | 2 | 117 | The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), laccase is 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 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 | 9.91e-44 | 27 | 607 | 3 | 535 | 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. |
400195 | Cu-oxidase_3 | 2.25e-41 | 29 | 143 | 3 | 119 | Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 620 | 1 | 620 | |
0.0 | 1 | 620 | 1 | 620 | |
0.0 | 1 | 620 | 1 | 620 | |
0.0 | 1 | 620 | 1 | 657 | |
3.71e-258 | 16 | 600 | 17 | 606 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.47e-40 | 34 | 597 | 16 | 471 | Crystal structure of laccase from Cerrena maxima at 1.76A resolution [Cerrena] |
|
7.02e-40 | 34 | 597 | 16 | 471 | Crystal structure of laccase from Cerrena maxima at 1.9A resolution [Trametes maxima] |
|
9.59e-40 | 26 | 595 | 8 | 469 | 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] |
|
9.59e-40 | 26 | 595 | 8 | 469 | Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta] |
|
1.79e-39 | 26 | 595 | 8 | 469 | Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.67e-274 | 14 | 600 | 15 | 607 | Laccase-1 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=yA PE=2 SV=3 |
|
2.45e-174 | 13 | 606 | 14 | 591 | Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1 |
|
9.34e-173 | 16 | 603 | 14 | 579 | Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1 |
|
3.40e-171 | 16 | 604 | 19 | 597 | Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1 |
|
2.30e-168 | 19 | 604 | 20 | 602 | Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000221 | 0.999754 | CS pos: 19-20. Pr: 0.9795 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.