Species | Magnaporthiopsis poae | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae | |||||||||||
CAZyme ID | KLU87092.1 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | SGNH_hydro domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0C4E149] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE3 | 31 | 230 | 4.3e-51 | 0.9948453608247423 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
238871 | XynB_like | 4.89e-34 | 31 | 230 | 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 | 1.72e-13 | 36 | 219 | 2 | 174 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
238141 | SGNH_hydrolase | 1.35e-10 | 36 | 228 | 4 | 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. |
395531 | Lipase_GDSL | 2.14e-09 | 33 | 226 | 1 | 224 | GDSL-like Lipase/Acylhydrolase. |
238881 | SGNH_hydrolase_like_6 | 3.70e-05 | 113 | 226 | 58 | 173 | 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 |
---|---|---|---|---|---|
9.58e-104 | 8 | 243 | 8 | 249 | |
6.32e-91 | 16 | 243 | 1 | 223 | |
1.04e-89 | 16 | 243 | 1 | 223 | |
3.45e-59 | 1 | 242 | 14 | 253 | |
5.89e-57 | 24 | 251 | 36 | 260 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.84e-09 | 31 | 227 | 6 | 192 | Chain A, LIPOLYTIC ENZYME [Acetivibrio thermocellus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.16e-06 | 19 | 241 | 32 | 266 | Multidomain esterase OS=Ruminococcus flavefaciens OX=1265 GN=cesA PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000611 | 0.999355 | CS pos: 23-24. Pr: 0.8095 |
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