Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1732; | |||||||||||
CAZyme ID | MGYG000003627_01517 | |||||||||||
CAZy Family | GH10 | |||||||||||
CAZyme Description | Endo-1,4-beta-xylanase B | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 728; End: 1840 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH10 | 36 | 360 | 1.1e-104 | 0.9834983498349835 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00331 | Glyco_hydro_10 | 2.78e-116 | 34 | 360 | 1 | 310 | Glycosyl hydrolase family 10. |
smart00633 | Glyco_10 | 6.47e-113 | 75 | 358 | 1 | 263 | Glycosyl hydrolase family 10. |
COG3693 | XynA | 1.91e-98 | 12 | 366 | 5 | 345 | Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]. |
cd17542 | REC_CheY | 0.008 | 188 | 266 | 37 | 100 | phosphoacceptor receiver (REC) domain of chemotaxis protein CheY. The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AFN75725.1 | 8.82e-98 | 11 | 363 | 3 | 369 |
ACW02028.1 | 4.57e-91 | 42 | 359 | 6 | 338 |
ACP87400.1 | 4.57e-91 | 42 | 359 | 6 | 338 |
ACW01955.1 | 4.51e-90 | 10 | 361 | 7 | 372 |
ACP87327.1 | 4.51e-90 | 10 | 361 | 7 | 372 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6FHE_A | 7.09e-81 | 28 | 359 | 7 | 339 | Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct] |
2Q8X_A | 3.13e-80 | 33 | 361 | 7 | 331 | Thehigh-resolution crystal structure of ixt6, a thermophilic, intracellular xylanase from G. stearothermophilus [unidentified],2Q8X_B The high-resolution crystal structure of ixt6, a thermophilic, intracellular xylanase from G. stearothermophilus [unidentified],3MSD_A Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MSD_B Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MSG_A Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MSG_B Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus] |
1N82_A | 1.76e-79 | 33 | 361 | 7 | 331 | Thehigh-resolution crystal structure of IXT6, a thermophilic, intracellular xylanase from G. stearothermophilus [Geobacillus stearothermophilus],1N82_B The high-resolution crystal structure of IXT6, a thermophilic, intracellular xylanase from G. stearothermophilus [Geobacillus stearothermophilus],3MUA_A Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MUA_B Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus] |
3MS8_A | 2.49e-79 | 33 | 361 | 7 | 331 | Enzyme-Substrateinteractions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MS8_B Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus] |
3MUI_A | 1.40e-78 | 33 | 361 | 7 | 331 | Enzyme-Substrateinteractions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MUI_B Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P48789 | 1.91e-79 | 1 | 361 | 1 | 367 | Endo-1,4-beta-xylanase A OS=Prevotella ruminicola OX=839 GN=xynA PE=3 SV=1 |
O69231 | 1.58e-77 | 42 | 359 | 16 | 329 | Endo-1,4-beta-xylanase B OS=Paenibacillus barcinonensis OX=198119 GN=xynB PE=1 SV=1 |
P49942 | 1.03e-74 | 11 | 365 | 8 | 375 | Endo-1,4-beta-xylanase A OS=Bacteroides ovatus OX=28116 GN=xylI PE=2 SV=1 |
P45703 | 1.87e-72 | 33 | 361 | 7 | 330 | Endo-1,4-beta-xylanase OS=Geobacillus stearothermophilus OX=1422 GN=xynA PE=1 SV=1 |
P23556 | 3.77e-72 | 31 | 359 | 18 | 340 | Endo-1,4-beta-xylanase A OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=xynA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000813 | 0.701028 | 0.297421 | 0.000282 | 0.000239 | 0.000197 |
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