| Species | Coprococcus sp900767685 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus sp900767685 | |||||||||||
| CAZyme ID | MGYG000000364_01864 | |||||||||||
| CAZy Family | CE17 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 51370; End: 52524 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE17 | 26 | 188 | 1.6e-71 | 0.9878787878787879 |
| CBM35inCE17 | 241 | 383 | 2.5e-59 | 0.9530201342281879 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd00229 | SGNH_hydrolase | 1.27e-19 | 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 | 2.41e-18 | 26 | 188 | 1 | 174 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| cd01834 | SGNH_hydrolase_like_2 | 6.27e-13 | 24 | 197 | 4 | 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. |
| COG2755 | TesA | 5.68e-08 | 23 | 204 | 10 | 213 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
| cd01827 | sialate_O-acetylesterase_like1 | 1.49e-07 | 24 | 197 | 3 | 185 | sialate O-acetylesterase_like family of the SGNH hydrolases, 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. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CBK82540.1 | 3.47e-266 | 1 | 384 | 1 | 384 |
| AXB29270.1 | 4.61e-170 | 1 | 384 | 1 | 359 |
| CBL01980.1 | 6.19e-168 | 1 | 384 | 1 | 359 |
| BCN32107.1 | 4.41e-109 | 5 | 382 | 16 | 368 |
| EEV02614.1 | 3.67e-108 | 6 | 382 | 17 | 367 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6HH9_A | 1.63e-109 | 6 | 382 | 17 | 367 | 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 | 9.26e-109 | 6 | 382 | 17 | 367 | 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 |
|---|---|---|---|---|---|
| 1.000053 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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