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CAZyme Information: GBF64245.1
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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 | Trichophyton mentagrophytes | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton mentagrophytes | |||||||||||
| CAZyme ID | GBF64245.1 | |||||||||||
| CAZy Family | GH47 | |||||||||||
| CAZyme Description | iron transport multicopper oxidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| AA1 | 149 | 650 | 1.5e-90 | 0.9804469273743017 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 274555 | ascorbase | 3.81e-72 | 135 | 649 | 4 | 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 | 1.63e-65 | 137 | 652 | 28 | 543 | L-ascorbate oxidase |
| 259977 | CuRO_3_MCO_like_4 | 7.29e-62 | 497 | 655 | 1 | 166 | 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. |
| 215324 | PLN02604 | 5.48e-60 | 136 | 649 | 28 | 540 | oxidoreductase |
| 225043 | SufI | 7.32e-54 | 128 | 657 | 29 | 450 | Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 1.61e-206 | 120 | 672 | 108 | 689 | |
| 2.14e-200 | 120 | 664 | 97 | 661 | |
| 8.83e-200 | 201 | 674 | 1 | 483 | |
| 9.17e-197 | 48 | 655 | 4 | 598 | |
| 1.31e-195 | 48 | 655 | 21 | 615 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3.39e-63 | 132 | 672 | 2 | 501 | Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae] |
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| 2.75e-57 | 131 | 651 | 64 | 538 | Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada] |
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| 7.23e-57 | 131 | 651 | 64 | 538 | 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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| 1.93e-52 | 101 | 653 | 17 | 530 | Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger] |
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| 4.21e-52 | 129 | 653 | 18 | 502 | Crystal structure of a laccase-like multicopper oxidase McoG from 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 |
|---|---|---|---|---|---|---|
| 8.38e-67 | 147 | 649 | 40 | 490 | 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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| 4.00e-66 | 132 | 671 | 19 | 521 | Iron transport multicopper oxidase FET3 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=FET3 PE=3 SV=1 |
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| 1.34e-64 | 132 | 671 | 27 | 526 | Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1 |
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| 7.74e-63 | 132 | 649 | 22 | 489 | Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1 |
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| 1.34e-61 | 132 | 672 | 23 | 522 | Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.998797 | 0.001216 |
