Species | Aspergillus sydowii | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus sydowii | |||||||||||
CAZyme ID | ASPSYDRAFT_211035-t33_1-p1 | |||||||||||
CAZy Family | GH146 | |||||||||||
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 | 39 | 630 | 5.9e-102 | 0.6196808510638298 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
236657 | PRK10150 | 0.0 | 39 | 636 | 2 | 597 | beta-D-glucuronidase; Provisional |
225789 | LacZ | 1.05e-105 | 44 | 634 | 7 | 598 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
397119 | Glyco_hydro_2_C | 3.01e-95 | 317 | 633 | 1 | 299 | Glycosyl hydrolases family 2, TIM barrel domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
236673 | ebgA | 1.55e-37 | 104 | 609 | 113 | 556 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
397120 | Glyco_hydro_2_N | 2.24e-25 | 51 | 216 | 3 | 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 | 637 | 1 | 639 | |
0.0 | 1 | 636 | 1 | 638 | |
0.0 | 1 | 634 | 1 | 631 | |
0.0 | 1 | 634 | 2 | 635 | |
0.0 | 1 | 633 | 1 | 630 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.91e-315 | 30 | 634 | 1 | 600 | The structure of Aspergillus oryzae beta-glucuronidase [Aspergillus oryzae],5C70_B The structure of Aspergillus oryzae beta-glucuronidase [Aspergillus oryzae] |
|
4.80e-315 | 15 | 634 | 11 | 625 | 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] |
|
5.39e-218 | 39 | 634 | 2 | 591 | Chain B, Beta-D-glucuronidase [Escherichia coli] |
|
5.58e-218 | 39 | 634 | 3 | 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] |
|
5.78e-218 | 39 | 634 | 4 | 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 |
---|---|---|---|---|---|---|
2.77e-217 | 39 | 634 | 2 | 591 | Beta-glucuronidase OS=Escherichia coli (strain K12) OX=83333 GN=uidA PE=1 SV=2 |
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8.57e-173 | 39 | 631 | 28 | 626 | Beta-glucuronidase OS=Homo sapiens OX=9606 GN=GUSB PE=1 SV=2 |
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1.94e-171 | 39 | 631 | 28 | 625 | Beta-glucuronidase OS=Canis lupus familiaris OX=9615 GN=GUSB PE=1 SV=1 |
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3.88e-171 | 39 | 631 | 28 | 626 | Beta-glucuronidase OS=Pongo abelii OX=9601 GN=GUSB PE=2 SV=2 |
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4.00e-171 | 39 | 631 | 29 | 626 | Beta-glucuronidase OS=Sus scrofa OX=9823 GN=GUSB PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000300 | 0.999681 | CS pos: 18-19. Pr: 0.9773 |
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