Species | CAG-510 sp900550475 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-510; CAG-510 sp900550475 | |||||||||||
CAZyme ID | MGYG000001965_00612 | |||||||||||
CAZy Family | CE17 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 28293; End: 29414 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE17 | 37 | 201 | 1.6e-77 | 0.9939393939393939 |
CBM35inCE17 | 228 | 372 | 2.5e-58 | 0.959731543624161 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00229 | SGNH_hydrolase | 5.16e-23 | 35 | 210 | 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 | 5.74e-21 | 37 | 202 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
cd01834 | SGNH_hydrolase_like_2 | 8.22e-17 | 35 | 209 | 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 | 5.15e-07 | 34 | 204 | 10 | 201 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
cd01822 | Lysophospholipase_L1_like | 1.94e-06 | 33 | 204 | 1 | 169 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AEN97394.1 | 7.44e-149 | 1 | 373 | 1 | 381 |
EEV02614.1 | 1.58e-144 | 1 | 371 | 1 | 367 |
CBL10432.1 | 5.21e-143 | 1 | 371 | 1 | 367 |
CBL12377.1 | 5.21e-143 | 1 | 371 | 1 | 367 |
BCN32107.1 | 1.44e-142 | 5 | 371 | 5 | 368 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6HH9_A | 7.11e-146 | 1 | 371 | 1 | 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 | 1.90e-143 | 5 | 371 | 5 | 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] |
1YZF_A | 3.30e-09 | 71 | 213 | 39 | 188 | Crystalstructure of the lipase/acylhydrolase from Enterococcus faecalis [Enterococcus faecalis V583] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000052 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.