Species | Podospora comata | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora comata | |||||||||||
CAZyme ID | VBB73737.1 | |||||||||||
CAZy Family | AA7 | |||||||||||
CAZyme Description | Putative Carbohydrate Esterase Family 5 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE5 | 29 | 222 | 1.6e-44 | 0.9788359788359788 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
395860 | Cutinase | 9.24e-46 | 27 | 223 | 1 | 173 | Cutinase. |
238382 | Lipase | 0.003 | 75 | 150 | 2 | 66 | 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 |
---|---|---|---|---|---|
3.60e-188 | 1 | 296 | 1 | 296 | |
4.68e-184 | 1 | 296 | 1 | 296 | |
4.68e-184 | 1 | 296 | 1 | 296 | |
2.68e-52 | 26 | 226 | 29 | 235 | |
2.76e-48 | 27 | 239 | 25 | 239 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.88e-24 | 31 | 224 | 5 | 207 | Chain A, ACETYL XYLAN ESTERASE [Trichoderma reesei],1QOZ_B Chain B, ACETYL XYLAN ESTERASE [Trichoderma reesei] |
|
6.01e-23 | 31 | 222 | 5 | 205 | Acetylxylan Esterase From P. Purpurogenum Refined At 1.10 Angstroms [Talaromyces purpureogenus] |
|
6.01e-23 | 31 | 222 | 5 | 205 | ACETYLXYLAN ESTERASE AT 0.90 ANGSTROM RESOLUTION [Talaromyces purpureogenus] |
|
8.48e-22 | 31 | 222 | 5 | 205 | Iodinated Complex Of Acetyl Xylan Esterase At 1.80 Angstroms [Talaromyces purpureogenus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.59e-27 | 6 | 225 | 4 | 231 | Cutinase 11 OS=Verticillium dahliae OX=27337 GN=VD0003_g7577 PE=1 SV=1 |
|
5.29e-23 | 31 | 225 | 36 | 239 | Acetylxylan esterase OS=Hypocrea jecorina OX=51453 GN=axe1 PE=1 SV=1 |
|
5.54e-22 | 31 | 222 | 32 | 232 | Acetylxylan esterase 2 OS=Talaromyces purpureogenus OX=1266744 GN=axe-2 PE=1 SV=1 |
|
6.87e-14 | 32 | 222 | 51 | 225 | Phospholipase Culp4 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=cut4 PE=1 SV=3 |
|
7.62e-11 | 3 | 225 | 19 | 228 | Probable carboxylesterase Culp3 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=cut3 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.997880 | 0.002181 |
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