Species | Bacteroides faecis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides faecis | |||||||||||
CAZyme ID | MGYG000002281_04937 | |||||||||||
CAZy Family | GH141 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 7623; End: 9992 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH141 | 32 | 486 | 1.5e-58 | 0.9184060721062619 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam13229 | Beta_helix | 2.23e-09 | 317 | 463 | 23 | 155 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
pfam13229 | Beta_helix | 2.75e-07 | 318 | 461 | 1 | 129 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
cd00987 | PDZ_serine_protease | 2.51e-06 | 710 | 786 | 14 | 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 | 8.59e-05 | 278 | 376 | 59 | 151 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
cd00991 | PDZ_archaeal_metalloprotease | 3.18e-04 | 735 | 782 | 25 | 72 | PDZ domain of archaeal zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AWW32784.1 | 3.93e-199 | 33 | 761 | 33 | 772 |
BAU63437.1 | 9.32e-40 | 54 | 567 | 93 | 593 |
AFZ35556.1 | 9.25e-37 | 54 | 666 | 84 | 710 |
AWV97657.1 | 1.90e-29 | 33 | 665 | 29 | 707 |
QZT37819.1 | 1.15e-28 | 16 | 666 | 8 | 719 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5MQP_A | 9.39e-17 | 34 | 455 | 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 |
---|---|---|---|---|---|
0.155225 | 0.833488 | 0.010177 | 0.000391 | 0.000322 | 0.000373 |
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