Species | Aspergillus luchuensis | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis | |||||||||||
CAZyme ID | ASPFODRAFT_202611-t33_1-p1 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | glycoside hydrolase family 2 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 | 1.2e-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 | 1.39e-107 | 1 | 592 | 1 | 596 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
397119 | Glyco_hydro_2_C | 2.64e-97 | 278 | 593 | 1 | 299 | Glycosyl hydrolases family 2, TIM barrel domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
236673 | ebgA | 3.30e-37 | 68 | 556 | 113 | 547 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
397120 | Glyco_hydro_2_N | 5.43e-26 | 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] |
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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] |
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1.93e-224 | 1 | 594 | 1 | 591 | Chain B, Beta-D-glucuronidase [Escherichia coli] |
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2.00e-224 | 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] |
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2.07e-224 | 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 |
---|---|---|---|---|---|---|
9.91e-224 | 1 | 594 | 1 | 591 | Beta-glucuronidase OS=Escherichia coli (strain K12) OX=83333 GN=uidA PE=1 SV=2 |
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5.04e-168 | 1 | 591 | 27 | 625 | Beta-glucuronidase OS=Felis catus OX=9685 GN=GUSB PE=1 SV=1 |
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3.67e-167 | 1 | 592 | 27 | 624 | Beta-glucuronidase OS=Mus musculus OX=10090 GN=Gusb PE=1 SV=2 |
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1.04e-166 | 1 | 592 | 27 | 624 | Beta-glucuronidase OS=Rattus norvegicus OX=10116 GN=Gusb PE=1 SV=1 |
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1.14e-166 | 1 | 591 | 27 | 625 | Beta-glucuronidase OS=Canis lupus familiaris OX=9615 GN=GUSB PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000052 | 0.000010 |
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