Species | Bacteroides caccae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides caccae | |||||||||||
CAZyme ID | MGYG000002549_02784 | |||||||||||
CAZy Family | GH141 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 66003; End: 68366 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH141 | 27 | 543 | 1.6e-63 | 0.9867172675521821 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00987 | PDZ_serine_protease | 3.73e-12 | 695 | 785 | 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 | 1.03e-08 | 674 | 787 | 233 | 338 | Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]. |
pfam13180 | PDZ_2 | 3.87e-07 | 715 | 787 | 3 | 74 | PDZ domain. |
smart00228 | PDZ | 6.80e-06 | 713 | 777 | 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 | 7.95e-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 | 7.52e-214 | 18 | 761 | 21 | 773 |
BAU63437.1 | 5.83e-43 | 41 | 669 | 79 | 733 |
QHT69676.1 | 3.40e-36 | 7 | 664 | 2 | 687 |
QJD84702.1 | 1.07e-35 | 27 | 566 | 33 | 611 |
AFZ35556.1 | 2.20e-35 | 26 | 664 | 47 | 710 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5MQP_A | 1.09e-18 | 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 |
---|---|---|---|---|---|
0.289926 | 0.697107 | 0.010026 | 0.000927 | 0.000652 | 0.001334 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.