Species | Fusarium verticillioides | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium verticillioides | |||||||||||
CAZyme ID | FVEG_11952-t26_1-p1 | |||||||||||
CAZy Family | GH62 | |||||||||||
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 | 485 | 683 | 3.2e-48 | 0.9948453608247423 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
238871 | XynB_like | 5.72e-51 | 485 | 683 | 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. |
238861 | SEST_like | 1.58e-30 | 52 | 331 | 1 | 238 | 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. |
404371 | Lipase_GDSL_2 | 6.15e-16 | 490 | 674 | 2 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
238141 | SGNH_hydrolase | 3.00e-11 | 487 | 682 | 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 | 2.36e-08 | 487 | 679 | 1 | 224 | GDSL-like Lipase/Acylhydrolase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 1438 | 1 | 1436 | |
0.0 | 1 | 1438 | 1 | 1437 | |
0.0 | 43 | 1438 | 43 | 1455 | |
0.0 | 453 | 1438 | 16 | 844 | |
0.0 | 468 | 1419 | 342 | 1309 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.65e-11 | 56 | 155 | 7 | 97 | Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297 [Streptomyces albidoflavus] |
|
7.51e-09 | 56 | 171 | 6 | 107 | 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] |
|
4.54e-08 | 850 | 1048 | 422 | 606 | Crystal Structure of TcdB2-TccC3-Cdc42 [Photorhabdus luminescens] |
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4.55e-08 | 850 | 1048 | 453 | 637 | Crystal Structure of TcdB2-TccC3 without hypervariable C-terminal region [Photorhabdus luminescens] |
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4.56e-08 | 850 | 1048 | 487 | 671 | Crystal Structure of TcdB2-TccC3 [Photorhabdus luminescens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.35e-08 | 56 | 236 | 40 | 179 | Lipase 1 OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=SCO1725 PE=1 SV=1 |
|
5.85e-08 | 56 | 171 | 40 | 141 | Lipase OS=Streptomyces rimosus OX=1927 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000280 | 0.999706 | CS pos: 19-20. Pr: 0.9742 |
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