Species | Blautia_A sp003471165 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A sp003471165 | |||||||||||
CAZyme ID | MGYG000000200_00675 | |||||||||||
CAZy Family | CE17 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 87463; End: 88539 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE17 | 26 | 189 | 2e-78 | 0.9939393939393939 |
CBM35inCE17 | 212 | 355 | 1.2e-63 | 0.959731543624161 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00229 | SGNH_hydrolase | 8.05e-23 | 24 | 198 | 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. |
pfam13472 | Lipase_GDSL_2 | 2.96e-21 | 26 | 190 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
cd01834 | SGNH_hydrolase_like_2 | 1.99e-13 | 26 | 195 | 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. |
COG2755 | TesA | 2.85e-12 | 23 | 205 | 10 | 214 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
pfam00657 | Lipase_GDSL | 3.64e-08 | 24 | 195 | 1 | 224 | GDSL-like Lipase/Acylhydrolase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBL01980.1 | 1.41e-183 | 1 | 358 | 1 | 359 |
AXB29270.1 | 2.71e-181 | 1 | 358 | 1 | 359 |
CBK82540.1 | 1.88e-173 | 1 | 358 | 1 | 384 |
BCN32107.1 | 8.50e-123 | 5 | 355 | 16 | 367 |
AEN97394.1 | 2.70e-120 | 5 | 358 | 16 | 381 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6HH9_A | 1.19e-120 | 6 | 355 | 17 | 366 | 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 | 1.57e-118 | 6 | 355 | 17 | 366 | 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 |
---|---|---|---|---|---|
1.000074 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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