Species | Fusarium oxysporum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum | |||||||||||
CAZyme ID | FOMG_05920-t38_1-p1 | |||||||||||
CAZy Family | CE5 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.11:4 | 3.2.1.57:2 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH49 | 25 | 598 | 4.1e-179 | 0.9872495446265938 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
407501 | Glyco_hydro_49N | 9.79e-62 | 25 | 212 | 7 | 185 | Glycosyl hydrolase family 49 N-terminal Ig-like domain. Family of dextranase (EC 3.2.1.11) and isopullulanase (EC 3.2.1.57). Dextranase hydrolyzes alpha-1,6-glycosidic bonds in dextran polymers. This domain corresponds to the N-terminal Ig-like fold. |
408611 | B_solenoid_dext | 2.52e-10 | 354 | 393 | 1 | 33 | Beta solenoid repeat from Dextranase. The crystal structures of Dex49A from Penicillium minioluteum and of ATCC9642 isopullulanase from Aspergillus niger include beta-solenoid repeats, sharing structural similarities. This Pfam entry includes a single repeat unit of the repeat regions. |
397674 | Glyco_hydro_49 | 3.32e-09 | 485 | 599 | 7 | 117 | Glycosyl hydrolase family 49. Family of dextranase (EC 3.2.1.11) and isopullulanase (EC 3.2.1.57). Dextranase hydrolyzes alpha-1,6-glycosidic bonds in dextran polymers. This domain corresponds to the C-terminal pectate lyase like domain. |
408554 | IPU_b_solenoid | 1.90e-06 | 428 | 460 | 1 | 33 | Isopullulanase beta-solenoid repeat. IPU and dextranase repeat unit includes three (or one long and one short) parallel beta-strands. The repeat region as a whole folds into a beta-helix, known as beta-solenoid. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 600 | 1 | 600 | |
0.0 | 1 | 599 | 1 | 599 | |
0.0 | 1 | 599 | 1 | 599 | |
0.0 | 1 | 599 | 1 | 599 | |
0.0 | 1 | 599 | 1 | 565 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.33e-189 | 26 | 599 | 12 | 573 | Dex49A from Penicillium minioluteum [Talaromyces minioluteus],1OGO_X Dex49A from Penicillium minioluteum complex with isomaltose [Talaromyces minioluteus] |
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1.45e-81 | 29 | 596 | 12 | 577 | Dextranase AoDex KQ11 [Pseudarthrobacter oxydans] |
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6.02e-74 | 29 | 525 | 15 | 480 | Crystal Structure of Isopullulanase from Aspergillus niger ATCC 9642 [Aspergillus niger],1WMR_B Crystal Structure of Isopullulanase from Aspergillus niger ATCC 9642 [Aspergillus niger],1X0C_A Improved Crystal Structure of Isopullulanase from Aspergillus niger ATCC 9642 [Aspergillus niger],1X0C_B Improved Crystal Structure of Isopullulanase from Aspergillus niger ATCC 9642 [Aspergillus niger],2Z8G_A Aspergillus niger ATCC9642 isopullulanase complexed with isopanose [Aspergillus niger],2Z8G_B Aspergillus niger ATCC9642 isopullulanase complexed with isopanose [Aspergillus niger] |
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8.41e-74 | 29 | 525 | 15 | 480 | Crystal structure of the N-glycan-deficient variant N448A of isopullulanase complexed with isopanose [Aspergillus niger],3WWG_B Crystal structure of the N-glycan-deficient variant N448A of isopullulanase complexed with isopanose [Aspergillus niger],3WWG_C Crystal structure of the N-glycan-deficient variant N448A of isopullulanase complexed with isopanose [Aspergillus niger],3WWG_D Crystal structure of the N-glycan-deficient variant N448A of isopullulanase complexed with isopanose [Aspergillus niger] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.16e-189 | 26 | 599 | 46 | 607 | Dextranase OS=Talaromyces minioluteus OX=28574 GN=DEX PE=1 SV=1 |
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3.84e-78 | 29 | 596 | 63 | 628 | Dextranase OS=Arthrobacter globiformis OX=1665 PE=3 SV=1 |
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1.51e-76 | 29 | 596 | 63 | 628 | Dextranase OS=Arthrobacter sp. (strain CB-8) OX=74565 PE=1 SV=1 |
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4.40e-73 | 29 | 525 | 30 | 495 | Isopullulanase OS=Aspergillus niger OX=5061 GN=ipuA PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.999317 | 0.000718 |
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