Species | Alistipes_A sp900539755 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900539755 | |||||||||||
CAZyme ID | MGYG000004468_00353 | |||||||||||
CAZy Family | GH141 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 434479; End: 436740 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH141 | 54 | 564 | 6.7e-112 | 0.9943074003795066 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam13229 | Beta_helix | 2.37e-15 | 368 | 582 | 1 | 156 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
pfam13229 | Beta_helix | 6.11e-11 | 454 | 584 | 2 | 110 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
pfam05048 | NosD | 2.20e-07 | 415 | 612 | 9 | 210 | Periplasmic copper-binding protein (NosD). NosD is a periplasmic protein which is thought to insert copper into the exported reductase apoenzyme (NosZ). This region forms a parallel beta helix domain. |
pfam13229 | Beta_helix | 0.001 | 514 | 584 | 1 | 64 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
pfam17161 | DUF5123 | 0.004 | 554 | 699 | 1 | 101 | Domain of unknown function (DUF5123). |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCG53796.1 | 0.0 | 32 | 722 | 16 | 702 |
QHT69676.1 | 1.80e-253 | 36 | 721 | 6 | 688 |
QDV64237.1 | 2.23e-188 | 69 | 721 | 31 | 687 |
BAY12871.1 | 5.85e-171 | 55 | 714 | 48 | 698 |
CCW33972.1 | 1.64e-159 | 35 | 719 | 3 | 678 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5MQP_A | 1.53e-49 | 56 | 566 | 28 | 587 | 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] |
3VST_A | 6.06e-07 | 54 | 160 | 2 | 95 | Thecomplex structure of XylC with Tris [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VST_B The complex structure of XylC with Tris [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VST_C The complex structure of XylC with Tris [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VST_D The complex structure of XylC with Tris [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSU_A The complex structure of XylC with xylobiose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSU_B The complex structure of XylC with xylobiose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSU_C The complex structure of XylC with xylobiose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSU_D The complex structure of XylC with xylobiose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSV_A The complex structure of XylC with xylose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSV_B The complex structure of XylC with xylose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSV_C The complex structure of XylC with xylose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3VSV_D The complex structure of XylC with xylose [Thermoanaerobacterium saccharolyticum JW/SL-YS485] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.484662 | 0.490757 | 0.022670 | 0.000907 | 0.000437 | 0.000555 |
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