Species | CAG-110 sp900549495 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-110; CAG-110 sp900549495 | |||||||||||
CAZyme ID | MGYG000003824_00473 | |||||||||||
CAZy Family | CE17 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 11613; End: 12704 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE17 | 34 | 192 | 1.1e-64 | 0.9878787878787879 |
CBM35inCE17 | 219 | 362 | 3.4e-59 | 0.959731543624161 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam13472 | Lipase_GDSL_2 | 3.51e-22 | 34 | 193 | 1 | 175 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
cd00229 | SGNH_hydrolase | 1.52e-20 | 32 | 202 | 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. |
cd01822 | Lysophospholipase_L1_like | 7.60e-13 | 30 | 204 | 1 | 177 | 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. |
cd01834 | SGNH_hydrolase_like_2 | 5.03e-10 | 34 | 199 | 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. |
cd01828 | sialate_O-acetylesterase_like2 | 7.47e-09 | 34 | 204 | 4 | 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 |
---|---|---|---|---|---|
BCN32107.1 | 9.12e-146 | 2 | 362 | 5 | 370 |
EEV02614.1 | 2.74e-140 | 2 | 362 | 5 | 369 |
CBL10432.1 | 9.02e-139 | 2 | 362 | 5 | 369 |
CBL12377.1 | 9.02e-139 | 2 | 362 | 5 | 369 |
AEN97394.1 | 6.58e-130 | 2 | 362 | 5 | 381 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6HH9_A | 1.23e-141 | 2 | 362 | 5 | 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 | 2.32e-139 | 2 | 362 | 5 | 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] |
7DDY_A | 6.30e-06 | 29 | 196 | 23 | 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] |
6LFB_A | 6.66e-06 | 31 | 124 | 3 | 92 | E.coli Thioesterase I mutant DG [Escherichia coli] |
6LFC_A | 6.92e-06 | 31 | 124 | 3 | 92 | E.coli Thioesterase I mutant DG [Escherichia coli],6LFC_B E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_C E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_D E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_E E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_F E. coli Thioesterase I mutant DG [Escherichia coli] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000040 | 0.000004 | 0.000003 | 0.000000 | 0.000000 | 0.000000 |
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