Species | Aspergillus tubingensis | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tubingensis | |||||||||||
CAZyme ID | ASPTUDRAFT_54299-t33_1-p1 | |||||||||||
CAZy Family | GT109 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.31:89 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 7 | 593 | 6.8e-100 | 0.6170212765957447 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
236657 | PRK10150 | 0.0 | 1 | 594 | 1 | 595 | beta-D-glucuronidase; Provisional |
225789 | LacZ | 4.64e-105 | 1 | 592 | 1 | 596 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
397119 | Glyco_hydro_2_C | 7.19e-99 | 278 | 593 | 1 | 299 | Glycosyl hydrolases family 2, TIM barrel domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
236673 | ebgA | 3.89e-37 | 68 | 556 | 113 | 547 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
397120 | Glyco_hydro_2_N | 7.05e-27 | 12 | 180 | 1 | 169 | Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 592 | 1 | 592 | |
0.0 | 1 | 592 | 1 | 592 | |
0.0 | 1 | 591 | 1 | 591 | |
0.0 | 1 | 591 | 1 | 591 | |
0.0 | 2 | 594 | 41 | 636 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
0.0 | 1 | 591 | 34 | 622 | The structure of Aspergillus oryzae a-glucuronidase complexed with glycyrrhetinic acid monoglucuronide [Aspergillus oryzae],5C71_B The structure of Aspergillus oryzae a-glucuronidase complexed with glycyrrhetinic acid monoglucuronide [Aspergillus oryzae],5C71_C The structure of Aspergillus oryzae a-glucuronidase complexed with glycyrrhetinic acid monoglucuronide [Aspergillus oryzae],5C71_D The structure of Aspergillus oryzae a-glucuronidase complexed with glycyrrhetinic acid monoglucuronide [Aspergillus oryzae] |
|
0.0 | 1 | 591 | 9 | 597 | The structure of Aspergillus oryzae beta-glucuronidase [Aspergillus oryzae],5C70_B The structure of Aspergillus oryzae beta-glucuronidase [Aspergillus oryzae] |
|
6.31e-223 | 1 | 594 | 1 | 591 | Chain B, Beta-D-glucuronidase [Escherichia coli] |
|
6.54e-223 | 1 | 594 | 2 | 592 | Chain A, Beta-D-glucuronidase [Escherichia coli],6LEG_B Chain B, Beta-D-glucuronidase [Escherichia coli],6LEG_C Chain C, Beta-D-glucuronidase [Escherichia coli],6LEG_D Chain D, Beta-D-glucuronidase [Escherichia coli],6LEL_A Chain A, Beta-D-glucuronidase [Escherichia coli],6LEL_B Chain B, Beta-D-glucuronidase [Escherichia coli] |
|
6.77e-223 | 1 | 594 | 3 | 593 | Crystal structure of full-length E. coli beta-glucuronidase [Escherichia coli K-12],3K46_B Crystal structure of full-length E. coli beta-glucuronidase [Escherichia coli K-12],3K4D_A Crystal structure of E. coli beta-glucuronidase with the glucaro-d-lactam inhibitor bound [Escherichia coli K-12],3K4D_B Crystal structure of E. coli beta-glucuronidase with the glucaro-d-lactam inhibitor bound [Escherichia coli K-12],6LEM_A Chain A, Beta-D-glucuronidase [Escherichia coli] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.25e-222 | 1 | 594 | 1 | 591 | Beta-glucuronidase OS=Escherichia coli (strain K12) OX=83333 GN=uidA PE=1 SV=2 |
|
3.57e-168 | 1 | 591 | 27 | 625 | Beta-glucuronidase OS=Felis catus OX=9685 GN=GUSB PE=1 SV=1 |
|
1.47e-166 | 1 | 592 | 27 | 624 | Beta-glucuronidase OS=Rattus norvegicus OX=10116 GN=Gusb PE=1 SV=1 |
|
6.46e-166 | 1 | 591 | 27 | 625 | Beta-glucuronidase OS=Canis lupus familiaris OX=9615 GN=GUSB PE=1 SV=1 |
|
1.83e-165 | 1 | 591 | 27 | 626 | Beta-glucuronidase OS=Pongo abelii OX=9601 GN=GUSB PE=2 SV=2 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000053 | 0.000008 |
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