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CAZyme Information: AN5320-T-p1
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Aspergillus nidulans | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus nidulans | |||||||||||
| CAZyme ID | AN5320-T-p1 | |||||||||||
| CAZy Family | GH35 | |||||||||||
| CAZyme Description | Has domain(s) with predicted hydrolase activity | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE2 | 165 | 371 | 1.7e-25 | 0.9808612440191388 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 238869 | Endoglucanase_E_like | 7.31e-58 | 164 | 374 | 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. |
| 404371 | Lipase_GDSL_2 | 4.74e-15 | 167 | 362 | 1 | 174 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| 238141 | SGNH_hydrolase | 5.93e-15 | 165 | 371 | 1 | 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. |
| 238865 | sialate_O-acetylesterase_like1 | 9.75e-06 | 232 | 368 | 42 | 182 | sialate O-acetylesterase_like family of the SGNH hydrolases, 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 Ser-His-Asp(Glu) triad found in other serine hydrolases. |
| 395531 | Lipase_GDSL | 1.97e-05 | 165 | 369 | 1 | 224 | GDSL-like Lipase/Acylhydrolase. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 6.95e-250 | 3 | 401 | 2 | 400 | |
| 1.28e-220 | 1 | 401 | 1 | 307 | |
| 1.28e-220 | 1 | 401 | 1 | 307 | |
| 2.21e-173 | 16 | 401 | 15 | 398 | |
| 2.21e-173 | 16 | 401 | 15 | 398 |
Swiss-Prot Hits help
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.000302 | 0.999652 | CS pos: 17-18. Pr: 0.9035 |