Species | Sporothrix brasiliensis | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix brasiliensis | |||||||||||
CAZyme ID | SPBR_04877-t41_1-p1 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH93 | 40 | 347 | 2.5e-68 | 0.9478827361563518 |
CBM66 | 415 | 575 | 8.7e-20 | 0.9612903225806452 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
271234 | Sialidase_non-viral | 5.80e-05 | 54 | 252 | 84 | 262 | 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 | 4.09e-04 | 57 | 258 | 155 | 323 | 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. |
214740 | VPS10 | 0.004 | 90 | 244 | 302 | 451 | VPS10 domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.10e-145 | 40 | 577 | 46 | 579 | |
1.13e-131 | 17 | 579 | 23 | 576 | |
3.78e-122 | 19 | 579 | 8 | 581 | |
2.98e-121 | 19 | 577 | 8 | 577 | |
2.98e-121 | 19 | 579 | 8 | 581 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.10e-37 | 30 | 375 | 16 | 344 | Chain A, Alpha-l-arabinofuranosidase [Fusarium graminearum] |
|
2.10e-37 | 30 | 375 | 16 | 344 | Chain A, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],5M1Z_A Chain A, Exo-1,5-alpha-L-arabinofuranobiosidase [Fusarium graminearum] |
|
4.24e-37 | 57 | 303 | 33 | 274 | 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] |
|
1.41e-36 | 30 | 375 | 16 | 344 | Chain A, ALPHA-L-ARABINOFURANOSIDASE [Fusarium graminearum] |
|
1.41e-36 | 30 | 375 | 16 | 344 | 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] |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.006732 | 0.993240 | CS pos: 23-24. Pr: 0.9602 |
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