Species | Aspergillus lentulus | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus | |||||||||||
CAZyme ID | GAQ12185.1 | |||||||||||
CAZy Family | GT62 | |||||||||||
CAZyme Description | SGNH_hydro domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0S7E7Z6] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE3 | 60 | 262 | 4.6e-60 | 0.9948453608247423 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
238861 | SEST_like | 5.81e-57 | 1223 | 1482 | 1 | 242 | SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST), a causal agent of the potato scab disease, which hydrolyzes a specific ester bond in suberin, a plant lipid. The tertiary fold of this enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxylic acid. |
238871 | XynB_like | 1.83e-46 | 60 | 262 | 1 | 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 | 5.57e-16 | 65 | 251 | 2 | 174 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
395531 | Lipase_GDSL | 2.38e-15 | 62 | 258 | 1 | 224 | GDSL-like Lipase/Acylhydrolase. |
238141 | SGNH_hydrolase | 3.02e-11 | 62 | 261 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 1578 | 1 | 1528 | |
0.0 | 1 | 1578 | 1 | 1528 | |
0.0 | 1 | 929 | 1 | 867 | |
0.0 | 48 | 930 | 49 | 921 | |
8.00e-261 | 30 | 930 | 37 | 906 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.82e-09 | 1225 | 1461 | 5 | 199 | Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297 [Streptomyces albidoflavus] |
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1.65e-07 | 1224 | 1381 | 3 | 145 | Crystal structure of extracelular lipase from Streptomyces rimosus at 1.7A resolution [Streptomyces rimosus],5MAL_B Crystal structure of extracelular lipase from Streptomyces rimosus at 1.7A resolution [Streptomyces rimosus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.88e-07 | 1218 | 1381 | 31 | 179 | Lipase OS=Streptomyces rimosus OX=1927 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000594 | 0.999373 | CS pos: 23-24. Pr: 0.9621 |
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