Species | Pyricularia oryzae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Pyriculariaceae; Pyricularia; Pyricularia oryzae | |||||||||||
CAZyme ID | mRNA_M_BR32_EuGene_00084461-p1 | |||||||||||
CAZy Family | GH18 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.1.1.74:3 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE5 | 71 | 237 | 6e-40 | 0.9735449735449735 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
395860 | Cutinase | 1.46e-46 | 71 | 238 | 2 | 171 | Cutinase. |
238382 | Lipase | 0.006 | 121 | 211 | 1 | 95 | 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 |
---|---|---|---|---|---|
2.84e-201 | 1 | 287 | 1 | 287 | |
1.01e-59 | 59 | 241 | 183 | 364 | |
1.01e-59 | 59 | 241 | 183 | 364 | |
1.01e-59 | 59 | 241 | 183 | 364 | |
1.12e-59 | 59 | 241 | 187 | 368 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.57e-45 | 71 | 241 | 79 | 248 | 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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7.80e-25 | 44 | 241 | 1 | 208 | Chain A, CUTINASE [Fusarium vanettenii],1CUW_B Chain B, CUTINASE [Fusarium vanettenii] |
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1.12e-23 | 44 | 241 | 1 | 208 | Chain A, CUTINASE [Fusarium vanettenii] |
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2.18e-23 | 44 | 241 | 1 | 208 | Chain A, CUTINASE [Fusarium vanettenii] |
|
5.90e-23 | 44 | 241 | 1 | 208 | Chain A, CUTINASE [Fusarium vanettenii] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.05e-54 | 65 | 242 | 24 | 202 | Cutinase OS=Botryotinia fuckeliana OX=40559 GN=cutA PE=1 SV=1 |
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2.62e-49 | 65 | 239 | 24 | 198 | Cutinase OS=Monilinia fructicola OX=38448 GN=CUT1 PE=2 SV=1 |
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2.21e-48 | 58 | 241 | 21 | 202 | Cutinase pbc1 OS=Pyrenopeziza brassicae OX=76659 GN=pbc1 PE=1 SV=1 |
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1.12e-44 | 71 | 241 | 79 | 248 | Cutinase OS=Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) OX=1344414 GN=M419DRAFT_76732 PE=1 SV=1 |
|
1.12e-44 | 71 | 241 | 79 | 248 | Cutinase OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=TRIREDRAFT_60489 PE=3 SV=2 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000662 | 0.999305 | CS pos: 21-22. Pr: 0.9750 |
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