Species | Scedosporium apiospermum | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum | |||||||||||
CAZyme ID | SAPIO_CDS2208-t41_1-p1 | |||||||||||
CAZy Family | CBM63 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA7 | 20 | 232 | 3.2e-58 | 0.4585152838427948 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
223354 | GlcD | 3.65e-29 | 18 | 345 | 18 | 349 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
396238 | FAD_binding_4 | 9.84e-27 | 32 | 169 | 1 | 139 | FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. |
273750 | pln_FAD_oxido | 9.45e-11 | 29 | 220 | 29 | 233 | plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown. |
215242 | PLN02441 | 9.72e-08 | 153 | 193 | 194 | 233 | cytokinin dehydrogenase |
273751 | FAD_lactone_ox | 1.16e-07 | 38 | 218 | 21 | 198 | sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.44e-21 | 30 | 201 | 18 | 189 | |
4.40e-20 | 30 | 200 | 46 | 215 | |
4.40e-20 | 30 | 200 | 46 | 215 | |
1.45e-19 | 30 | 200 | 46 | 215 | |
6.10e-19 | 2 | 198 | 247 | 440 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.32e-16 | 32 | 197 | 48 | 214 | Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens] |
|
8.32e-16 | 32 | 197 | 48 | 214 | Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens] |
|
2.05e-15 | 7 | 198 | 38 | 226 | Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1] |
|
1.30e-14 | 18 | 233 | 71 | 287 | Chain A, MaDA-3 [Morus alba],7E2V_B Chain B, MaDA-3 [Morus alba] |
|
1.58e-14 | 12 | 187 | 25 | 198 | Chain A, Glucooligosaccharide oxidase [Sarocladium strictum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.28e-42 | 15 | 410 | 19 | 395 | FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1 |
|
7.01e-34 | 12 | 404 | 19 | 392 | FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1 |
|
3.33e-32 | 5 | 226 | 9 | 228 | FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1 |
|
3.08e-31 | 5 | 226 | 9 | 228 | FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1 |
|
2.20e-17 | 32 | 209 | 126 | 313 | FAD-linked oxidoreductase penH OS=Penicillium thymicola OX=293382 GN=penH PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000064 | 0.000000 |
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