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CAZyme Information: CVL03914.1
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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 | Fusarium mangiferae | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium mangiferae | |||||||||||
| CAZyme ID | CVL03914.1 | |||||||||||
| CAZy Family | GH5 | |||||||||||
| CAZyme Description | unspecified product | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE5 | 68 | 180 | 1.5e-21 | 0.6243386243386243 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 395860 | Cutinase | 1.11e-25 | 68 | 180 | 1 | 110 | Cutinase. |
| 225176 | PldB | 0.005 | 133 | 172 | 91 | 134 | Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]. |
| 238382 | Lipase | 0.007 | 138 | 162 | 17 | 41 | Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 1.50e-123 | 1 | 181 | 1 | 181 | |
| 1.50e-123 | 1 | 181 | 1 | 181 | |
| 1.50e-123 | 1 | 181 | 1 | 181 | |
| 2.03e-69 | 1 | 180 | 1 | 183 | |
| 1.23e-44 | 1 | 180 | 1 | 187 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 8.66e-17 | 64 | 180 | 74 | 187 | Structure of cutinase from Trichoderma reesei in its native form. [Trichoderma reesei QM6a],4PSD_A Structure of Trichoderma reesei cutinase native form. [Trichoderma reesei QM6a],4PSE_A Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor [Trichoderma reesei QM6a],4PSE_B Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor [Trichoderma reesei QM6a] |
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| 8.96e-11 | 59 | 179 | 19 | 142 | Chain A, CUTINASE [Fusarium vanettenii] |
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| 6.83e-09 | 61 | 164 | 16 | 119 | Chain A, cutinase [Malbranchea cinnamomea] |
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| 5.12e-06 | 61 | 162 | 7 | 111 | Crystal structure of a biodegradable plastic-degrading cutinase from Paraphoma sp. B47-9. [Paraphoma sp. B47-9],7CY3_B Crystal structure of a biodegradable plastic-degrading cutinase from Paraphoma sp. B47-9. [Paraphoma sp. B47-9],7CY9_A Crystal structure of a biodegradable plastic-degrading cutinase from Paraphoma sp. B47-9 solved by getting the phase from anomalous scattering of uncovalently coordinated arsenic (cacodylate). [Paraphoma sp. B47-9],7CY9_B Crystal structure of a biodegradable plastic-degrading cutinase from Paraphoma sp. B47-9 solved by getting the phase from anomalous scattering of uncovalently coordinated arsenic (cacodylate). [Paraphoma sp. B47-9] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6.86e-23 | 7 | 180 | 11 | 177 | Cutinase OS=Blumeria hordei OX=2867405 GN=CUT1 PE=3 SV=1 |
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| 2.71e-20 | 59 | 181 | 31 | 152 | Cutinase CUT2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=CUT2 PE=1 SV=1 |
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| 3.17e-19 | 69 | 178 | 31 | 138 | Cutinase OS=Botryotinia fuckeliana OX=40559 GN=cutA PE=1 SV=1 |
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| 1.94e-16 | 64 | 178 | 26 | 139 | Cutinase pbc1 OS=Pyrenopeziza brassicae OX=76659 GN=pbc1 PE=1 SV=1 |
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| 2.76e-16 | 59 | 171 | 50 | 158 | Cutinase 4 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=cut4 PE=2 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.000274 | 0.999688 | CS pos: 23-24. Pr: 0.6615 |