Species | Aspergillus brasiliensis | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus brasiliensis | |||||||||||
CAZyme ID | ASPBRDRAFT_40579-t33_1-p1 | |||||||||||
CAZy Family | GH43 | |||||||||||
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 | 38 | 618 | 1.4e-99 | 0.6090425531914894 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
236657 | PRK10150 | 0.0 | 35 | 627 | 1 | 594 | beta-D-glucuronidase; Provisional |
225789 | LacZ | 3.85e-106 | 35 | 626 | 1 | 596 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
397119 | Glyco_hydro_2_C | 1.04e-93 | 312 | 627 | 1 | 299 | Glycosyl hydrolases family 2, TIM barrel domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
236673 | ebgA | 3.69e-38 | 102 | 588 | 113 | 545 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
397120 | Glyco_hydro_2_N | 6.93e-25 | 46 | 214 | 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 | 35 | 625 | 1 | 591 | |
0.0 | 35 | 626 | 1 | 592 | |
0.0 | 35 | 626 | 1 | 592 | |
0.0 | 35 | 625 | 1 | 591 | |
0.0 | 1 | 625 | 1 | 633 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
0.0 | 30 | 625 | 29 | 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 | 34 | 625 | 8 | 597 | The structure of Aspergillus oryzae beta-glucuronidase [Aspergillus oryzae],5C70_B The structure of Aspergillus oryzae beta-glucuronidase [Aspergillus oryzae] |
|
6.36e-219 | 35 | 625 | 1 | 588 | Chain B, Beta-D-glucuronidase [Escherichia coli] |
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6.59e-219 | 35 | 625 | 2 | 589 | 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] |
|
6.82e-219 | 35 | 625 | 3 | 590 | 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 |
---|---|---|---|---|---|---|
3.27e-218 | 35 | 625 | 1 | 588 | Beta-glucuronidase OS=Escherichia coli (strain K12) OX=83333 GN=uidA PE=1 SV=2 |
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1.80e-165 | 28 | 626 | 20 | 624 | Beta-glucuronidase OS=Rattus norvegicus OX=10116 GN=Gusb PE=1 SV=1 |
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2.54e-165 | 35 | 626 | 27 | 624 | Beta-glucuronidase OS=Mus musculus OX=10090 GN=Gusb PE=1 SV=2 |
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5.59e-165 | 35 | 625 | 27 | 625 | Beta-glucuronidase OS=Canis lupus familiaris OX=9615 GN=GUSB PE=1 SV=1 |
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1.12e-164 | 32 | 625 | 24 | 625 | Beta-glucuronidase OS=Felis catus OX=9685 GN=GUSB PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000301 | 0.999675 | CS pos: 18-19. Pr: 0.9568 |
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