Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; ; | |||||||||||
CAZyme ID | MGYG000000456_01432 | |||||||||||
CAZy Family | CE1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1021; End: 2043 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE1 | 41 | 243 | 9.8e-30 | 0.6123348017621145 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG4099 | COG4099 | 8.74e-48 | 31 | 263 | 159 | 387 | Predicted peptidase [General function prediction only]. |
cd14256 | Dockerin_I | 1.20e-12 | 271 | 324 | 2 | 55 | Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex. |
COG3509 | LpqC | 5.69e-12 | 39 | 213 | 41 | 205 | Poly(3-hydroxybutyrate) depolymerase [Secondary metabolites biosynthesis, transport and catabolism]. |
TIGR01840 | esterase_phb | 4.03e-09 | 47 | 187 | 1 | 129 | esterase, PHB depolymerase family. This model describes a subfamily among lipases of the ab-hydrolase family. This subfamily includes bacterial depolymerases for poly(3-hydroxybutyrate) (PHB) and related polyhydroxyalkanoates (PHA), as well as acetyl xylan esterases, feruloyl esterases, and others from fungi. [Fatty acid and phospholipid metabolism, Degradation] |
COG0627 | FrmB | 4.85e-08 | 39 | 190 | 29 | 189 | S-formylglutathione hydrolase FrmB [Defense mechanisms]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCI61582.1 | 5.44e-53 | 31 | 264 | 810 | 1044 |
QDU56037.1 | 3.30e-34 | 36 | 263 | 790 | 1007 |
ABS60377.1 | 3.35e-34 | 43 | 263 | 20 | 245 |
ACR12533.1 | 3.10e-32 | 45 | 261 | 64 | 279 |
QJW99051.1 | 1.02e-26 | 25 | 263 | 27 | 240 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3DOH_A | 1.31e-52 | 42 | 263 | 155 | 380 | CrystalStructure of a Thermostable Esterase [Thermotoga maritima],3DOH_B Crystal Structure of a Thermostable Esterase [Thermotoga maritima],3DOI_A Crystal Structure of a Thermostable Esterase complex with paraoxon [Thermotoga maritima],3DOI_B Crystal Structure of a Thermostable Esterase complex with paraoxon [Thermotoga maritima] |
3WYD_A | 2.72e-25 | 42 | 263 | 18 | 217 | C-terminalesterase domain of LC-Est1 [uncultured organism],3WYD_B C-terminal esterase domain of LC-Est1 [uncultured organism] |
4Q82_A | 2.87e-12 | 62 | 263 | 81 | 277 | CrystalStructure of Phospholipase/Carboxylesterase from Haliangium ochraceum [Haliangium ochraceum DSM 14365],4Q82_B Crystal Structure of Phospholipase/Carboxylesterase from Haliangium ochraceum [Haliangium ochraceum DSM 14365] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B8YG19 | 7.98e-06 | 37 | 212 | 50 | 203 | Bifunctional acetylxylan esterase/xylanase XynS20E OS=Neocallimastix patriciarum OX=4758 GN=xynS20E PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000467 | 0.400445 | 0.598609 | 0.000175 | 0.000152 | 0.000137 |
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