Species | Sporothrix schenckii | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii | |||||||||||
CAZyme ID | SPSK_00548-t39_1-p1 | |||||||||||
CAZy Family | AA2 | |||||||||||
CAZyme Description | glycoside hydrolase family 93 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH93 | 43 | 347 | 1.3e-109 | 0.993485342019544 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
271234 | Sialidase_non-viral | 8.13e-05 | 49 | 257 | 149 | 336 | 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 | 0.009 | 48 | 162 | 202 | 305 | 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 |
---|---|---|---|---|---|
5.20e-149 | 27 | 372 | 18 | 369 | |
6.64e-148 | 8 | 368 | 8 | 376 | |
6.64e-148 | 8 | 368 | 8 | 376 | |
2.44e-145 | 8 | 368 | 8 | 375 | |
1.27e-143 | 28 | 368 | 20 | 368 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.30e-144 | 27 | 372 | 10 | 365 | Chain A, Alpha-l-arabinofuranosidase [Fusarium graminearum] |
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7.45e-144 | 27 | 372 | 10 | 365 | Chain A, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],5M1Z_A Chain A, Exo-1,5-alpha-L-arabinofuranobiosidase [Fusarium graminearum] |
|
6.06e-143 | 27 | 372 | 10 | 365 | 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] |
|
9.91e-142 | 27 | 371 | 10 | 364 | Chain A, ALPHA-L-ARABINOFURANOSIDASE [Fusarium graminearum] |
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1.91e-131 | 22 | 372 | 1 | 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 |
---|---|---|
0.053948 | 0.946008 | CS pos: 20-21. Pr: 0.8530 |
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