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CAZyme Information: MGYG000000184_01608
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Blautia_A luti | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A luti | |||||||||||
| CAZyme ID | MGYG000000184_01608 | |||||||||||
| CAZy Family | CE17 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 43179; End: 44255 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE17 | 26 | 189 | 1.3e-78 | 0.9939393939393939 |
| CBM35inCE17 | 212 | 357 | 2.9e-64 | 0.9731543624161074 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd00229 | SGNH_hydrolase | 3.86e-23 | 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 | 7.76e-21 | 26 | 190 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| COG2755 | TesA | 2.22e-12 | 23 | 207 | 10 | 216 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
| cd01834 | SGNH_hydrolase_like_2 | 4.21e-12 | 26 | 195 | 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. |
| pfam00657 | Lipase_GDSL | 7.15e-09 | 24 | 195 | 1 | 224 | GDSL-like Lipase/Acylhydrolase. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CBL01980.1 | 2.45e-184 | 1 | 358 | 1 | 359 |
| AXB29270.1 | 4.70e-182 | 1 | 358 | 1 | 359 |
| CBK82540.1 | 1.40e-175 | 1 | 358 | 1 | 384 |
| BCN32107.1 | 2.98e-123 | 5 | 356 | 16 | 368 |
| CBL10432.1 | 1.64e-120 | 6 | 356 | 17 | 367 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6HH9_A | 2.95e-121 | 6 | 356 | 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 | 9.63e-120 | 6 | 356 | 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] |
Swiss-Prot Hits help
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000061 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |