Species | Parabacteroides timonensis | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides timonensis | |||||||||||
CAZyme ID | MGYG000001591_04094 | |||||||||||
CAZy Family | GH141 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 6152; End: 8524 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH141 | 26 | 542 | 9.8e-59 | 0.9867172675521821 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00987 | PDZ_serine_protease | 7.92e-08 | 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. |
pfam13229 | Beta_helix | 1.58e-05 | 422 | 584 | 1 | 156 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
COG0265 | DegQ | 2.98e-04 | 711 | 784 | 263 | 336 | Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]. |
pfam13180 | PDZ_2 | 2.99e-04 | 715 | 784 | 3 | 72 | PDZ domain. |
smart00228 | PDZ | 0.003 | 701 | 775 | 9 | 83 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AWW32784.1 | 4.12e-220 | 16 | 760 | 21 | 773 |
BAU63437.1 | 1.62e-40 | 47 | 639 | 88 | 695 |
AWV97657.1 | 1.58e-34 | 6 | 663 | 3 | 707 |
AQQ71020.1 | 3.73e-33 | 22 | 652 | 19 | 698 |
AFZ35556.1 | 3.91e-33 | 53 | 664 | 90 | 710 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5MQP_A | 7.97e-15 | 23 | 496 | 23 | 608 | 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 |
---|---|---|---|---|---|
0.000333 | 0.998865 | 0.000242 | 0.000187 | 0.000185 | 0.000186 |
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