Species | Alternaria alternata | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata | |||||||||||
CAZyme ID | OAG15987.1 | |||||||||||
CAZy Family | AA9 | |||||||||||
CAZyme Description | cutinase-domain-containing protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE5 | 77 | 249 | 3.5e-42 | 0.9894179894179894 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
395860 | Cutinase | 1.56e-48 | 77 | 235 | 1 | 157 | Cutinase. |
238382 | Lipase | 0.002 | 132 | 219 | 2 | 94 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
8.55e-148 | 1 | 250 | 1 | 250 | |
3.53e-131 | 20 | 249 | 20 | 249 | |
2.13e-129 | 7 | 250 | 5 | 248 | |
2.27e-91 | 7 | 250 | 4 | 248 | |
3.99e-91 | 1 | 250 | 1 | 245 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.33e-38 | 73 | 246 | 74 | 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] |
|
1.35e-23 | 59 | 235 | 5 | 183 | Chain A, cutinase [Malbranchea cinnamomea] |
|
9.85e-21 | 66 | 244 | 3 | 185 | Humicola insolens cutinase [Humicola insolens],4OYY_B Humicola insolens cutinase [Humicola insolens],4OYY_C Humicola insolens cutinase [Humicola insolens],4OYY_D Humicola insolens cutinase [Humicola insolens],4OYY_E Humicola insolens cutinase [Humicola insolens],4OYY_F Humicola insolens cutinase [Humicola insolens],4OYY_G Humicola insolens cutinase [Humicola insolens],4OYY_H Humicola insolens cutinase [Humicola insolens],4OYY_I Humicola insolens cutinase [Humicola insolens],4OYY_J Humicola insolens cutinase [Humicola insolens],4OYY_K Humicola insolens cutinase [Humicola insolens],4OYY_L Humicola insolens cutinase [Humicola insolens] |
|
1.47e-20 | 59 | 250 | 5 | 196 | Crystal structure of Aspergillus oryzae cutinase [Aspergillus oryzae] |
|
2.37e-19 | 70 | 250 | 5 | 187 | Structure of Aspergillus oryzae cutinase expressed in Pichia pastoris, crystallized in the presence of Paraoxon [Aspergillus oryzae] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.88e-46 | 74 | 246 | 27 | 196 | Cutinase OS=Botryotinia fuckeliana OX=40559 GN=cutA PE=1 SV=1 |
|
9.78e-46 | 59 | 250 | 22 | 214 | Cutinase CUT2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=CUT2 PE=1 SV=1 |
|
3.77e-45 | 74 | 246 | 27 | 195 | Cutinase OS=Monilinia fructicola OX=38448 GN=CUT1 PE=2 SV=1 |
|
2.29e-43 | 68 | 250 | 58 | 236 | Cutinase OS=Blumeria hordei OX=2867405 GN=CUT1 PE=3 SV=1 |
|
1.42e-42 | 78 | 249 | 32 | 200 | Cutinase pbc1 OS=Pyrenopeziza brassicae OX=76659 GN=pbc1 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000216 | 0.999737 | CS pos: 20-21. Pr: 0.9864 |
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