Species | Pyricularia oryzae | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Pyriculariaceae; Pyricularia; Pyricularia oryzae | |||||||||||
CAZyme ID | mRNA_M_BR32_EuGene_00037001-p1 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE3 | 23 | 212 | 4.5e-52 | 0.9639175257731959 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
238871 | XynB_like | 8.98e-39 | 23 | 218 | 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 | 3.83e-15 | 28 | 206 | 2 | 173 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
238141 | SGNH_hydrolase | 4.68e-12 | 28 | 217 | 4 | 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 | 5.10e-09 | 26 | 211 | 2 | 221 | GDSL-like Lipase/Acylhydrolase. |
238879 | NnaC_like | 3.49e-08 | 76 | 168 | 28 | 122 | NnaC (CMP-NeuNAc synthetase) _like subfamily of 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 two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
4.35e-168 | 1 | 231 | 1 | 231 | |
4.53e-78 | 3 | 228 | 10 | 235 | |
5.62e-74 | 22 | 227 | 30 | 235 | |
3.60e-73 | 20 | 227 | 85 | 292 | |
3.60e-73 | 20 | 227 | 85 | 292 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.83e-72 | 23 | 225 | 2 | 206 | Crystal structure of a carbohydrate esterase family 3 from Talaromyces cellulolyticus [Talaromyces cellulolyticus] |
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1.38e-71 | 23 | 225 | 2 | 206 | Crystal structure of acetyl esterase mutant S10A with acetate ion [Talaromyces cellulolyticus] |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000245 | 0.999731 | CS pos: 19-20. Pr: 0.9807 |
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