| Species | CAG-882 sp000435595 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-882; CAG-882 sp000435595 | |||||||||||
| CAZyme ID | MGYG000004369_00739 | |||||||||||
| CAZy Family | CE17 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 101088; End: 102275 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE17 | 40 | 203 | 2.1e-75 | 0.9939393939393939 |
| CBM35inCE17 | 247 | 391 | 1.8e-66 | 0.9664429530201343 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd00229 | SGNH_hydrolase | 4.44e-19 | 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. |
| pfam13472 | Lipase_GDSL_2 | 1.44e-18 | 40 | 204 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| cd01834 | SGNH_hydrolase_like_2 | 5.84e-16 | 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. |
| cd04501 | SGNH_hydrolase_like_4 | 1.59e-07 | 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. |
| COG2755 | TesA | 3.11e-05 | 37 | 216 | 10 | 211 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| EEV02614.1 | 1.53e-162 | 8 | 395 | 5 | 372 |
| CBL10432.1 | 5.07e-161 | 8 | 395 | 5 | 372 |
| CBL12377.1 | 5.07e-161 | 8 | 395 | 5 | 372 |
| AEN97394.1 | 1.41e-159 | 8 | 395 | 5 | 384 |
| BCN32107.1 | 1.22e-139 | 8 | 390 | 5 | 368 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6HH9_A | 6.93e-164 | 8 | 395 | 5 | 372 | 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 | 6.53e-162 | 8 | 395 | 5 | 372 | 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] |
| 1YZF_A | 2.48e-07 | 38 | 214 | 4 | 187 | Crystalstructure of the lipase/acylhydrolase from Enterococcus faecalis [Enterococcus faecalis V583] |
| 1IVN_A | 2.59e-06 | 37 | 224 | 3 | 185 | E.coliThioesterase I/Protease I/Lysophospholiase L1 [Escherichia coli],1U8U_A E. coli Thioesterase I/Protease I/Lysophospholiase L1 in complexed with octanoic acid [Escherichia coli] |
| 1JRL_A | 2.59e-06 | 37 | 224 | 3 | 185 | ChainA, Acyl-CoA Thioesterase I [Escherichia coli],1V2G_A Chain A, Acyl-CoA thioesterase I [Escherichia coli] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P0ADA1 | 9.64e-06 | 29 | 218 | 23 | 205 | Thioesterase 1/protease 1/lysophospholipase L1 OS=Escherichia coli (strain K12) OX=83333 GN=tesA PE=1 SV=1 |
| P0ADA2 | 9.64e-06 | 29 | 218 | 23 | 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 |
|---|---|---|---|---|---|
| 1.000065 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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