Species | Roseburia sp900753715 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia sp900753715 | |||||||||||
CAZyme ID | MGYG000003892_02567 | |||||||||||
CAZy Family | CE17 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 3569; End: 4690 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE17 | 37 | 200 | 4.5e-79 | 0.9939393939393939 |
CBM35inCE17 | 229 | 373 | 1.2e-68 | 0.9664429530201343 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00229 | SGNH_hydrolase | 3.65e-21 | 35 | 206 | 1 | 184 | 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 | 2.45e-20 | 37 | 201 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
cd01834 | SGNH_hydrolase_like_2 | 2.32e-14 | 37 | 206 | 6 | 188 | 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. |
cd01822 | Lysophospholipase_L1_like | 1.16e-09 | 38 | 203 | 6 | 169 | Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity. |
cd04501 | SGNH_hydrolase_like_4 | 2.35e-08 | 37 | 206 | 5 | 179 | 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 | 4.49e-201 | 1 | 373 | 1 | 369 |
CBL10432.1 | 1.49e-199 | 1 | 373 | 1 | 369 |
CBL12377.1 | 1.49e-199 | 1 | 373 | 1 | 369 |
AEN97394.1 | 8.46e-184 | 1 | 373 | 1 | 381 |
BCN32107.1 | 2.02e-159 | 1 | 373 | 1 | 370 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6HH9_A | 2.04e-202 | 1 | 373 | 1 | 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 | 9.17e-199 | 3 | 373 | 3 | 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] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000060 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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