| Species | Bacteroides sp900555635 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900555635 | |||||||||||
| CAZyme ID | MGYG000004899_01443 | |||||||||||
| CAZy Family | GH141 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 122622; End: 124991 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH141 | 29 | 550 | 1.2e-56 | 0.9867172675521821 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd00987 | PDZ_serine_protease | 7.76e-08 | 704 | 787 | 4 | 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 | 8.72e-07 | 697 | 785 | 245 | 334 | Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]. |
| pfam13229 | Beta_helix | 4.38e-05 | 320 | 470 | 23 | 157 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
| pfam13180 | PDZ_2 | 0.002 | 726 | 786 | 7 | 71 | PDZ domain. |
| pfam13229 | Beta_helix | 0.004 | 429 | 573 | 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 | 3.14e-222 | 1 | 786 | 3 | 794 |
| BAU63437.1 | 5.99e-49 | 25 | 671 | 53 | 729 |
| AFZ35556.1 | 2.68e-47 | 26 | 671 | 45 | 711 |
| AWV97657.1 | 8.47e-38 | 1 | 669 | 1 | 707 |
| BAY12871.1 | 8.21e-37 | 26 | 667 | 45 | 701 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5MQP_A | 1.66e-20 | 29 | 459 | 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 |
|---|---|---|---|---|---|
| 0.000497 | 0.998558 | 0.000394 | 0.000179 | 0.000162 | 0.000157 |
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