Species | Aspergillus terreus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus terreus | |||||||||||
CAZyme ID | ATEG_02797-t26_1-p1 | |||||||||||
CAZy Family | GH1 | |||||||||||
CAZyme Description | conserved hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE3 | 28 | 215 | 3.7e-51 | 0.9432989690721649 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
238871 | XynB_like | 1.43e-46 | 77 | 215 | 14 | 150 | SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are 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. |
404371 | Lipase_GDSL_2 | 8.53e-14 | 29 | 210 | 1 | 173 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
238141 | SGNH_hydrolase | 1.71e-12 | 27 | 221 | 1 | 187 | 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. |
395531 | Lipase_GDSL | 1.12e-08 | 27 | 215 | 1 | 221 | GDSL-like Lipase/Acylhydrolase. |
238872 | SGNH_hydrolase_like_2 | 7.62e-08 | 27 | 218 | 4 | 188 | SGNH_hydrolase subfamily. SGNH hydrolases are 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
8.90e-141 | 1 | 228 | 1 | 224 | |
1.33e-134 | 1 | 230 | 1 | 225 | |
3.73e-127 | 1 | 230 | 1 | 226 | |
3.73e-127 | 1 | 230 | 1 | 226 | |
3.73e-127 | 1 | 230 | 1 | 226 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.47e-135 | 29 | 228 | 6 | 205 | Crystal structure of a carbohydrate esterase family 3 from Talaromyces cellulolyticus [Talaromyces cellulolyticus] |
|
9.94e-135 | 29 | 228 | 6 | 205 | Crystal structure of acetyl esterase mutant S10A with acetate ion [Talaromyces cellulolyticus] |
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2.04e-17 | 30 | 215 | 11 | 188 | Chain A, LIPOLYTIC ENZYME [Acetivibrio thermocellus] |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000265 | 0.999727 | CS pos: 20-21. Pr: 0.7916 |
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