Species | CAG-882 sp003486385 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-882; CAG-882 sp003486385 | |||||||||||
CAZyme ID | MGYG000002609_01088 | |||||||||||
CAZy Family | CE17 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 7990; End: 9159 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE17 | 40 | 203 | 6.8e-75 | 0.9939393939393939 |
CBM35inCE17 | 243 | 387 | 1.3e-64 | 0.9664429530201343 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam13472 | Lipase_GDSL_2 | 3.28e-19 | 40 | 204 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
cd00229 | SGNH_hydrolase | 1.26e-18 | 38 | 211 | 1 | 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. |
cd01834 | SGNH_hydrolase_like_2 | 1.03e-15 | 40 | 211 | 6 | 190 | 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. |
PRK10528 | PRK10528 | 5.33e-06 | 29 | 214 | 6 | 184 | multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional |
cd04501 | SGNH_hydrolase_like_4 | 9.19e-06 | 40 | 213 | 5 | 183 | Members of the SGNH-hydrolase superfamily, 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 from other serine hydrolases, but may lack the carboxlic acid. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
EEV02614.1 | 2.69e-159 | 8 | 387 | 5 | 369 |
CBL10432.1 | 2.19e-158 | 8 | 387 | 5 | 369 |
CBL12377.1 | 2.19e-158 | 8 | 387 | 5 | 369 |
AEN97394.1 | 9.95e-156 | 8 | 388 | 5 | 382 |
BCN32107.1 | 9.09e-143 | 8 | 387 | 5 | 370 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6HH9_A | 1.21e-160 | 8 | 387 | 5 | 369 | Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82] |
6HFZ_A | 1.14e-158 | 8 | 387 | 5 | 369 | Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82] |
6LFB_A | 4.81e-07 | 37 | 218 | 3 | 179 | E.coli Thioesterase I mutant DG [Escherichia coli] |
6LFC_A | 5.02e-07 | 37 | 218 | 3 | 179 | E.coli Thioesterase I mutant DG [Escherichia coli],6LFC_B E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_C E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_D E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_E E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_F E. coli Thioesterase I mutant DG [Escherichia coli] |
5TIC_A | 5.24e-07 | 37 | 218 | 6 | 182 | X-raystructure of wild-type E. coli Acyl-CoA thioesterase I at pH 5 [Escherichia coli],5TIC_B X-ray structure of wild-type E. coli Acyl-CoA thioesterase I at pH 5 [Escherichia coli] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0ADA1 | 3.85e-06 | 37 | 218 | 29 | 205 | Thioesterase 1/protease 1/lysophospholipase L1 OS=Escherichia coli (strain K12) OX=83333 GN=tesA PE=1 SV=1 |
P0ADA2 | 3.85e-06 | 37 | 218 | 29 | 205 | Thioesterase 1/protease 1/lysophospholipase L1 OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=tesA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000061 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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