Species | Magnaporthiopsis poae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae | |||||||||||
CAZyme ID | KLU91347.1 | |||||||||||
CAZy Family | GT1 | |||||||||||
CAZyme Description | glycosyl hydrolase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH33 | 29 | 373 | 1.3e-18 | 0.8859649122807017 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
404074 | BNR_2 | 1.69e-60 | 39 | 371 | 1 | 280 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
227036 | COG4692 | 1.58e-56 | 27 | 385 | 32 | 371 | Predicted neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
271234 | Sialidase_non-viral | 1.16e-41 | 22 | 385 | 8 | 338 | 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 |
---|---|---|---|---|---|
7.01e-214 | 2 | 391 | 5 | 395 | |
4.15e-134 | 18 | 388 | 24 | 383 | |
4.15e-134 | 18 | 388 | 24 | 383 | |
4.15e-134 | 18 | 388 | 24 | 383 | |
1.11e-133 | 8 | 388 | 11 | 381 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000009 | 0.000048 |
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