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CAZyme Information: MGYG000000695_00204
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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 | Prevotella sp000436035 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000436035 | |||||||||||
| CAZyme ID | MGYG000000695_00204 | |||||||||||
| CAZy Family | CE3 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 77341; End: 78702 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE3 | 23 | 210 | 2.5e-42 | 0.979381443298969 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd01833 | XynB_like | 1.27e-25 | 21 | 211 | 1 | 157 | SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. 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. |
| COG0657 | Aes | 1.11e-17 | 194 | 447 | 21 | 310 | Acetyl esterase/lipase [Lipid transport and metabolism]. |
| cd00229 | SGNH_hydrolase | 1.98e-14 | 26 | 209 | 4 | 186 | 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 | 2.69e-14 | 26 | 199 | 2 | 173 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| COG2755 | TesA | 1.39e-11 | 22 | 219 | 10 | 216 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BAX78799.1 | 7.72e-124 | 17 | 450 | 34 | 494 |
| ATC65549.1 | 4.60e-109 | 11 | 450 | 28 | 492 |
| QOV88633.1 | 8.69e-70 | 19 | 215 | 28 | 226 |
| QNN20991.1 | 1.25e-58 | 17 | 215 | 26 | 226 |
| AFZ21551.1 | 7.28e-29 | 19 | 223 | 38 | 248 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5AO9_A | 1.33e-26 | 215 | 453 | 6 | 281 | Thestructure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-native [Thermogutta terrifontis],5AOA_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-Propionate bound [Thermogutta terrifontis],5AOB_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-butyrate bound [Thermogutta terrifontis],5AOC_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-valerate bound [Thermogutta terrifontis] |
| 7BFN_A | 1.36e-26 | 215 | 453 | 7 | 282 | ChainA, Esterase [Thermogutta terrifontis] |
| 7BFO_A | 6.65e-26 | 215 | 453 | 7 | 282 | ChainA, Esterase [Thermogutta terrifontis],7BFR_A Chain A, Esterase [Thermogutta terrifontis],7BFT_A Chain A, Esterase [Thermogutta terrifontis],7BFU_A Chain A, Esterase [Thermogutta terrifontis],7BFV_A Chain A, Esterase [Thermogutta terrifontis] |
| 2C7B_A | 1.93e-07 | 234 | 364 | 56 | 183 | TheCrystal Structure of EstE1, a New Thermophilic and Thermostable Carboxylesterase Cloned from a Metagenomic Library [uncultured archaeon],2C7B_B The Crystal Structure of EstE1, a New Thermophilic and Thermostable Carboxylesterase Cloned from a Metagenomic Library [uncultured archaeon] |
Swiss-Prot Hits help
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000392 | 0.998878 | 0.000172 | 0.000187 | 0.000173 | 0.000162 |