| Species | Prevotellamassilia sp900772575 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia; Prevotellamassilia sp900772575 | |||||||||||
| CAZyme ID | MGYG000003674_01053 | |||||||||||
| CAZy Family | GH141 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 1186; End: 3582 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH141 | 29 | 481 | 5.3e-56 | 0.9089184060721063 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd00987 | PDZ_serine_protease | 1.80e-12 | 696 | 786 | 1 | 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. |
| pfam13180 | PDZ_2 | 4.20e-07 | 717 | 786 | 3 | 72 | PDZ domain. |
| smart00228 | PDZ | 1.64e-06 | 703 | 778 | 9 | 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. |
| COG0265 | DegQ | 2.96e-06 | 713 | 786 | 263 | 336 | Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]. |
| pfam13229 | Beta_helix | 2.78e-05 | 317 | 463 | 23 | 155 | 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 | 1.21e-203 | 31 | 787 | 34 | 796 |
| BAU63437.1 | 3.30e-37 | 31 | 642 | 58 | 695 |
| QNN21980.1 | 1.09e-34 | 31 | 665 | 24 | 672 |
| AFZ35556.1 | 1.73e-34 | 31 | 667 | 49 | 711 |
| CCW33972.1 | 1.51e-30 | 16 | 665 | 18 | 678 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5MQP_A | 5.14e-13 | 30 | 455 | 27 | 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 |
|---|---|---|---|---|---|
| 0.009113 | 0.320226 | 0.666451 | 0.002241 | 0.001113 | 0.000824 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.