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CAZyme Information: EJT46677.1
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Trichosporon asahii | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Basidiomycota; Tremellomycetes; ; Trichosporonaceae; Trichosporon; Trichosporon asahii | |||||||||||
| CAZyme ID | EJT46677.1 | |||||||||||
| CAZy Family | CBM13 | |||||||||||
| CAZyme Description | Multicopper oxidase [Source:UniProtKB/TrEMBL;Acc:J6EV61] | |||||||||||
| CAZyme Property |
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CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| AA1 | 138 | 656 | 1.3e-75 | 0.8435754189944135 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 259953 | CuRO_2_MCO_like_1 | 1.74e-64 | 227 | 427 | 1 | 162 | The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs 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. |
| 259977 | CuRO_3_MCO_like_4 | 6.59e-59 | 484 | 660 | 1 | 164 | The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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. |
| 274555 | ascorbase | 1.27e-49 | 108 | 656 | 1 | 517 | 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. |
| 177843 | PLN02191 | 1.04e-46 | 138 | 669 | 88 | 553 | L-ascorbate oxidase |
| 215324 | PLN02604 | 8.62e-36 | 100 | 656 | 17 | 540 | oxidoreductase |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 1.62e-102 | 102 | 680 | 92 | 604 | |
| 5.66e-93 | 102 | 681 | 109 | 619 | |
| 5.94e-86 | 23 | 665 | 22 | 597 | |
| 3.97e-74 | 8 | 681 | 26 | 681 | |
| 7.95e-71 | 61 | 681 | 87 | 685 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7.53e-36 | 109 | 680 | 24 | 522 | Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger] |
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| 7.62e-36 | 109 | 680 | 25 | 523 | Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger] |
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| 7.79e-36 | 100 | 681 | 59 | 562 | Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada] |
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| 1.41e-35 | 100 | 681 | 59 | 562 | Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada] |
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| 1.85e-35 | 109 | 680 | 52 | 550 | Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2.89e-50 | 108 | 667 | 73 | 556 | Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1 |
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| 1.03e-46 | 108 | 697 | 22 | 528 | Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1 |
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| 3.49e-43 | 141 | 692 | 96 | 527 | Iron transport multicopper oxidase fio1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=fio1 PE=3 SV=1 |
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| 3.37e-41 | 101 | 697 | 17 | 532 | 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 |
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| 7.01e-41 | 112 | 697 | 24 | 535 | Multicopper oxidase abr1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr1 PE=2 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.999973 | 0.000063 |
