Species | Bacteroides sp900761785 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900761785 | |||||||||||
CAZyme ID | MGYG000003252_05760 | |||||||||||
CAZy Family | GH141 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 19332; End: 21692 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH141 | 27 | 293 | 1.1e-43 | 0.5370018975332068 |
GH141 | 306 | 543 | 1.6e-17 | 0.38519924098671726 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00987 | PDZ_serine_protease | 6.44e-13 | 695 | 784 | 2 | 90 | PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins. |
COG0265 | DegQ | 7.86e-09 | 675 | 786 | 234 | 338 | Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]. |
pfam13180 | PDZ_2 | 4.93e-07 | 715 | 783 | 3 | 70 | PDZ domain. |
smart00228 | PDZ | 1.69e-06 | 713 | 776 | 21 | 84 | Domain present in PSD-95, Dlg, and ZO-1/2. Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities. |
pfam13229 | Beta_helix | 6.14e-06 | 422 | 566 | 1 | 137 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AWW32784.1 | 4.59e-209 | 18 | 760 | 21 | 773 |
BAU63437.1 | 4.86e-41 | 38 | 669 | 80 | 733 |
AWV97657.1 | 4.65e-38 | 10 | 663 | 5 | 707 |
QJD84702.1 | 1.46e-36 | 27 | 566 | 33 | 611 |
QNN21980.1 | 7.76e-35 | 27 | 679 | 23 | 687 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5MQP_A | 2.83e-16 | 28 | 452 | 28 | 501 | Glycosidehydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_B Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_C Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_D Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_E Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_F Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_G Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_H Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.194451 | 0.797130 | 0.006115 | 0.000976 | 0.000544 | 0.000764 |
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