Species | Gaeumannomyces tritici | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Magnaporthaceae; Gaeumannomyces; Gaeumannomyces tritici | |||||||||||
CAZyme ID | EJT73738.1 | |||||||||||
CAZy Family | GH125 | |||||||||||
CAZyme Description | BNR/Asp-box repeat domain-containing protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH93 | 43 | 349 | 1.3e-97 | 0.9869706840390879 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
271234 | Sialidase_non-viral | 1.64e-06 | 51 | 159 | 153 | 251 | Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases. |
271234 | Sialidase_non-viral | 0.001 | 49 | 154 | 205 | 302 | Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.43e-191 | 25 | 378 | 28 | 382 | |
6.58e-170 | 25 | 380 | 57 | 420 | |
7.73e-166 | 23 | 378 | 28 | 386 | |
7.73e-166 | 23 | 378 | 28 | 386 | |
7.73e-166 | 23 | 378 | 28 | 386 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.86e-93 | 28 | 370 | 10 | 360 | Chain A, Alpha-l-arabinofuranosidase [Fusarium graminearum] |
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9.73e-93 | 28 | 370 | 10 | 360 | Chain A, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],5M1Z_A Chain A, Exo-1,5-alpha-L-arabinofuranobiosidase [Fusarium graminearum] |
|
7.78e-92 | 28 | 370 | 10 | 360 | Chain A, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],2YDP_B Chain B, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],2YDP_C Chain C, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum] |
|
6.21e-91 | 28 | 370 | 10 | 360 | Chain A, ALPHA-L-ARABINOFURANOSIDASE [Fusarium graminearum] |
|
5.55e-77 | 33 | 373 | 10 | 355 | High resolution structure of Penicillium chrysogenum alpha-L-arabinanase [Penicillium chrysogenum],3A72_A High resolution structure of Penicillium chrysogenum alpha-L-arabinanase complexed with arabinobiose [Penicillium chrysogenum] |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.979884 | 0.020145 |
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