Species | Roseburia sp003483745 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia sp003483745 | |||||||||||
CAZyme ID | MGYG000000546_01603 | |||||||||||
CAZy Family | CE17 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 5970; End: 7088 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE17 | 37 | 200 | 3.3e-79 | 0.9939393939393939 |
CBM35inCE17 | 222 | 369 | 7e-71 | 0.9865771812080537 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00229 | SGNH_hydrolase | 2.91e-23 | 35 | 209 | 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. |
cd01834 | SGNH_hydrolase_like_2 | 9.17e-20 | 34 | 206 | 3 | 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. |
pfam13472 | Lipase_GDSL_2 | 2.23e-19 | 37 | 201 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
COG2755 | TesA | 6.14e-09 | 35 | 203 | 11 | 201 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
cd01828 | sialate_O-acetylesterase_like2 | 5.13e-08 | 34 | 211 | 1 | 169 | sialate_O-acetylesterase_like subfamily 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 |
---|---|---|---|---|---|
EEV02614.1 | 6.92e-260 | 1 | 372 | 1 | 372 |
CBL10432.1 | 2.31e-258 | 1 | 372 | 1 | 372 |
CBL12377.1 | 2.31e-258 | 1 | 372 | 1 | 372 |
AEN97394.1 | 6.21e-174 | 1 | 372 | 1 | 384 |
BCN32107.1 | 5.79e-173 | 1 | 369 | 1 | 370 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6HH9_A | 3.17e-261 | 1 | 372 | 1 | 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 | 8.32e-257 | 2 | 372 | 2 | 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] |
7DDY_A | 1.39e-07 | 31 | 203 | 22 | 213 | ChainA, G-D-S-L family lipolytic protein [Arcticibacterium luteifluviistationis],7DDY_B Chain B, G-D-S-L family lipolytic protein [Arcticibacterium luteifluviistationis],7DDY_C Chain C, G-D-S-L family lipolytic protein [Arcticibacterium luteifluviistationis],7DDY_D Chain D, G-D-S-L family lipolytic protein [Arcticibacterium luteifluviistationis] |
4OAO_A | 7.40e-07 | 28 | 203 | 2 | 204 | Amutant of Axe2 (R55A), and acetyl-xylooligosaccharide esterase from Geobacillus Stearmophilus [Geobacillus stearothermophilus],4OAO_B A mutant of Axe2 (R55A), and acetyl-xylooligosaccharide esterase from Geobacillus Stearmophilus [Geobacillus stearothermophilus] |
4OAP_A | 7.40e-07 | 28 | 203 | 2 | 204 | AnAxe2 mutant (W190I), an acetyl-xylooligosaccharide esterase from Geobacillus Stearmophilus [Geobacillus stearothermophilus],4OAP_B An Axe2 mutant (W190I), an acetyl-xylooligosaccharide esterase from Geobacillus Stearmophilus [Geobacillus stearothermophilus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q09LX1 | 5.46e-06 | 28 | 203 | 2 | 204 | Acetylxylan esterase OS=Geobacillus stearothermophilus OX=1422 GN=axe2 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000063 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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