Species | Aspergillus terreus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus terreus | |||||||||||
CAZyme ID | ATEG_08627-t26_1-p1 | |||||||||||
CAZy Family | GT15 | |||||||||||
CAZyme Description | conserved hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE2 | 179 | 372 | 6.7e-20 | 0.861244019138756 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
238869 | Endoglucanase_E_like | 1.25e-50 | 165 | 375 | 1 | 169 | Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
238141 | SGNH_hydrolase | 2.41e-12 | 233 | 372 | 44 | 186 | SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. |
404371 | Lipase_GDSL_2 | 3.99e-09 | 168 | 363 | 1 | 174 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
395531 | Lipase_GDSL | 0.007 | 245 | 370 | 68 | 224 | GDSL-like Lipase/Acylhydrolase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
5.11e-179 | 1 | 401 | 1 | 407 | |
2.26e-169 | 18 | 401 | 17 | 402 | |
3.14e-166 | 6 | 401 | 7 | 409 | |
4.29e-159 | 1 | 401 | 1 | 379 | |
5.50e-158 | 18 | 401 | 17 | 392 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.002300 | 0.997668 | CS pos: 19-20. Pr: 0.9697 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.