Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; | |||||||||||
CAZyme ID | MGYG000004180_03706 | |||||||||||
CAZy Family | CE17 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 8624; End: 10576 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE17 | 305 | 471 | 1e-16 | 0.9878787878787879 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam13472 | Lipase_GDSL_2 | 1.14e-13 | 305 | 472 | 1 | 175 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
cd00229 | SGNH_hydrolase | 6.54e-13 | 303 | 478 | 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. |
cd01834 | SGNH_hydrolase_like_2 | 1.89e-06 | 302 | 373 | 3 | 73 | 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. |
pfam00561 | Abhydrolase_1 | 1.90e-06 | 76 | 170 | 10 | 110 | alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. |
COG1506 | DAP2 | 1.11e-05 | 79 | 272 | 412 | 616 | Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AEE54090.1 | 2.56e-152 | 38 | 648 | 394 | 1015 |
QEC52777.1 | 6.55e-83 | 277 | 648 | 816 | 1251 |
BAV07942.1 | 6.84e-66 | 274 | 649 | 22 | 394 |
AHF91789.1 | 5.92e-28 | 285 | 608 | 40 | 377 |
AXT62271.1 | 2.03e-21 | 285 | 647 | 36 | 394 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6HH9_A | 2.85e-15 | 303 | 619 | 35 | 353 | 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 | 9.08e-15 | 303 | 619 | 35 | 353 | 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 |
---|---|---|---|---|---|
0.004992 | 0.994201 | 0.000247 | 0.000190 | 0.000162 | 0.000168 |
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