Species | Scedosporium apiospermum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum | |||||||||||
CAZyme ID | SAPIO_CDS8591-t41_1-p1 | |||||||||||
CAZy Family | GT17 | |||||||||||
CAZyme Description | Bnr asp-box repeat domain protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH93 | 54 | 363 | 3.5e-103 | 0.993485342019544 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
271234 | Sialidase_non-viral | 5.64e-05 | 46 | 272 | 71 | 278 | 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 | 6.50e-05 | 34 | 267 | 120 | 335 | 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 |
---|---|---|---|---|---|
4.61e-144 | 38 | 388 | 58 | 408 | |
5.10e-143 | 38 | 389 | 18 | 370 | |
2.21e-139 | 17 | 389 | 11 | 380 | |
3.61e-138 | 17 | 389 | 11 | 380 | |
3.61e-138 | 17 | 389 | 11 | 380 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.55e-139 | 38 | 389 | 10 | 366 | Chain A, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],5M1Z_A Chain A, Exo-1,5-alpha-L-arabinofuranobiosidase [Fusarium graminearum] |
|
8.90e-139 | 38 | 389 | 10 | 366 | Chain A, Alpha-l-arabinofuranosidase [Fusarium graminearum] |
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1.26e-138 | 38 | 389 | 10 | 366 | 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] |
|
1.18e-136 | 38 | 389 | 10 | 366 | Chain A, ALPHA-L-ARABINOFURANOSIDASE [Fusarium graminearum] |
|
8.94e-121 | 41 | 388 | 8 | 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 |
---|---|---|
0.000591 | 0.999360 | CS pos: 22-23. Pr: 0.9506 |
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