Species | Coprinopsis cinerea | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea | |||||||||||
CAZyme ID | CC1G_09365-t26_1-p1 | |||||||||||
CAZy Family | GH5 | |||||||||||
CAZyme Description | triacylglycerol lipase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE5 | 46 | 215 | 3.4e-39 | 0.9841269841269841 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
395860 | Cutinase | 9.81e-43 | 46 | 216 | 2 | 173 | Cutinase. |
238382 | Lipase | 4.64e-04 | 105 | 161 | 8 | 64 | 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. |
402661 | DUF2974 | 0.002 | 126 | 163 | 85 | 122 | Protein of unknown function (DUF2974). This bacterial family of proteins has no known function. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.00e-62 | 39 | 216 | 23 | 200 | |
1.11e-61 | 11 | 216 | 5 | 199 | |
4.01e-43 | 39 | 213 | 22 | 194 | |
4.91e-43 | 38 | 216 | 24 | 215 | |
1.58e-37 | 46 | 216 | 76 | 251 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.41e-34 | 40 | 212 | 73 | 243 | 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] |
|
9.78e-21 | 40 | 216 | 17 | 198 | Chain A, cutinase [Malbranchea cinnamomea] |
|
1.47e-17 | 37 | 201 | 22 | 191 | Chain A, CUTINASE [Fusarium vanettenii] |
|
5.54e-17 | 37 | 201 | 22 | 191 | Chain A, CUTINASE [Fusarium vanettenii] |
|
7.71e-17 | 37 | 201 | 22 | 191 | Chain A, CUTINASE [Fusarium vanettenii] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.97e-62 | 11 | 216 | 5 | 199 | Cutinase CUT1 OS=Coprinopsis cinerea OX=5346 GN=CUT1 PE=1 SV=1 |
|
1.30e-36 | 39 | 212 | 26 | 195 | Cutinase OS=Monilinia fructicola OX=38448 GN=CUT1 PE=2 SV=1 |
|
2.65e-36 | 39 | 212 | 26 | 196 | Cutinase OS=Botryotinia fuckeliana OX=40559 GN=cutA PE=1 SV=1 |
|
1.07e-33 | 40 | 212 | 73 | 243 | Cutinase OS=Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) OX=1344414 GN=M419DRAFT_76732 PE=1 SV=1 |
|
1.07e-33 | 40 | 212 | 73 | 243 | Cutinase OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=TRIREDRAFT_60489 PE=3 SV=2 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000219 | 0.999731 | CS pos: 18-19. Pr: 0.9797 |
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