You are browsing environment: FUNGIDB
CAZyme Information: KAG2008815.1
You are here: Home > Sequence: KAG2008815.1
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 | Coprinopsis cinerea | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea | |||||||||||
| CAZyme ID | KAG2008815.1 | |||||||||||
| CAZy Family | CE4 | |||||||||||
| CAZyme Description | cutinase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE5 | 31 | 200 | 3.6e-39 | 0.9841269841269841 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 395860 | Cutinase | 6.31e-44 | 31 | 201 | 2 | 173 | Cutinase. |
| 238382 | Lipase | 1.31e-04 | 93 | 187 | 7 | 108 | 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 |
|---|---|---|---|---|---|
| 2.11e-144 | 1 | 201 | 1 | 200 | |
| 8.79e-72 | 1 | 201 | 1 | 199 | |
| 1.54e-45 | 1 | 197 | 1 | 196 | |
| 1.87e-45 | 1 | 201 | 1 | 197 | |
| 5.93e-43 | 1 | 201 | 1 | 215 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.40e-31 | 25 | 201 | 73 | 247 | 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] |
|
| 7.06e-20 | 25 | 201 | 17 | 198 | Chain A, cutinase [Malbranchea cinnamomea] |
|
| 2.04e-17 | 23 | 201 | 13 | 196 | Crystal structure of Aspergillus oryzae cutinase [Aspergillus oryzae] |
|
| 8.89e-17 | 23 | 201 | 4 | 187 | Structure of Aspergillus oryzae cutinase expressed in Pichia pastoris, crystallized in the presence of Paraoxon [Aspergillus oryzae] |
|
| 3.94e-16 | 31 | 194 | 17 | 185 | 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 |
|---|---|---|---|---|---|---|
| 1.56e-72 | 1 | 201 | 1 | 199 | Cutinase CUT1 OS=Coprinopsis cinerea OX=5346 GN=CUT1 PE=1 SV=1 |
|
| 1.10e-42 | 1 | 197 | 1 | 195 | Cutinase OS=Monilinia fructicola OX=38448 GN=CUT1 PE=2 SV=1 |
|
| 2.31e-39 | 16 | 197 | 17 | 196 | Cutinase OS=Botryotinia fuckeliana OX=40559 GN=cutA PE=1 SV=1 |
|
| 5.33e-35 | 8 | 201 | 17 | 201 | Cutinase pbc1 OS=Pyrenopeziza brassicae OX=76659 GN=pbc1 PE=1 SV=1 |
|
| 1.40e-33 | 17 | 201 | 46 | 236 | Cutinase OS=Blumeria hordei OX=2867405 GN=CUT1 PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.000213 | 0.999774 | CS pos: 27-28. Pr: 0.4429 |