Species | Scedosporium apiospermum | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum | |||||||||||
CAZyme ID | SAPIO_CDS4087-t41_1-p1 | |||||||||||
CAZy Family | GH125 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE3 | 1 | 192 | 5.7e-58 | 0.9690721649484536 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
238871 | XynB_like | 5.47e-57 | 40 | 194 | 7 | 157 | 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 | 1.43e-23 | 2 | 185 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
238141 | SGNH_hydrolase | 1.85e-22 | 2 | 188 | 3 | 182 | 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 | 6.44e-16 | 1 | 190 | 2 | 224 | GDSL-like Lipase/Acylhydrolase. |
238868 | XynE_like | 3.29e-12 | 1 | 188 | 3 | 198 | SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen anaerobe Prevotella bryantii XynE. The P. bryantii XynE gene is located in a xylanase gene cluster. 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 |
---|---|---|---|---|---|
5.44e-93 | 1 | 199 | 48 | 246 | |
2.74e-90 | 1 | 198 | 175 | 372 | |
1.03e-89 | 1 | 198 | 35 | 232 | |
1.27e-89 | 1 | 198 | 160 | 354 | |
1.68e-89 | 1 | 198 | 49 | 246 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.20e-38 | 1 | 199 | 5 | 204 | Crystal structure of a carbohydrate esterase family 3 from Talaromyces cellulolyticus [Talaromyces cellulolyticus] |
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3.38e-38 | 1 | 199 | 5 | 204 | Crystal structure of acetyl esterase mutant S10A with acetate ion [Talaromyces cellulolyticus] |
|
2.43e-09 | 3 | 200 | 11 | 201 | Chain A, LIPOLYTIC ENZYME [Acetivibrio thermocellus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.59e-16 | 1 | 200 | 47 | 266 | Multidomain esterase OS=Ruminococcus flavefaciens OX=1265 GN=cesA PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.999987 | 0.000057 |
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