Species | Aspergillus lentulus | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus | |||||||||||
CAZyme ID | GAQ03950.1 | |||||||||||
CAZy Family | AA9 | |||||||||||
CAZyme Description | 4-dimethylallyltryptophan N-methyltransferase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA7 | 122 | 310 | 1.3e-48 | 0.3864628820960699 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
274580 | methyl_EasF | 1.72e-147 | 588 | 913 | 1 | 319 | probable methyltransferase domain, EasF family. This model represents an uncharacterized domain of about 300 amino acids with homology to S-adenosylmethionine-dependent methyltransferases. Proteins with this domain are exclusively fungal. A few, such as EasF from Neotyphodium lolii, are associated with the biosynthesis of ergot alkaloids, a class of fungal secondary metabolites. EasF may, in fact, be the AdoMet:dimethylallyltryptophan N-methyltransferase, the enzyme that follows tryptophan dimethylallyltransferase (DMATS) in ergot alkaloid biosynthesis. Several other members of this family, including mug158 (meiotically up-regulated gene 158 protein) from Schizosaccharomyces pombe, contain an additional uncharacterized domain DUF323 (pfam03781). |
401848 | Methyltransf_33 | 2.88e-87 | 600 | 915 | 1 | 304 | Histidine-specific methyltransferase, SAM-dependent. The mycobacterial members of this family are expressed from part of the ergothioneine biosynthetic gene cluster. EGTD is the histidine methyltransferase that transfers three methyl groups to the alpha-amino moiety of histidine, in the first stage of the production of this histidine betaine derivative that carries a thiol group attached to the C2 atom of an imidazole ring. |
226751 | COG4301 | 2.11e-29 | 604 | 910 | 22 | 315 | Uncharacterized conserved protein, contains predicted SAM-dependent methyltransferase domain [General function prediction only]. |
396238 | FAD_binding_4 | 1.11e-22 | 123 | 270 | 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. |
223354 | GlcD | 7.70e-14 | 113 | 281 | 23 | 186 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
6.06e-42 | 21 | 573 | 495 | 1054 | |
6.06e-42 | 21 | 573 | 495 | 1054 | |
1.33e-14 | 115 | 298 | 264 | 439 | |
2.30e-14 | 121 | 298 | 270 | 439 | |
3.07e-14 | 123 | 568 | 62 | 489 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.02e-69 | 25 | 576 | 27 | 566 | Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464] |
|
1.65e-42 | 23 | 575 | 27 | 589 | Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464] |
|
1.90e-17 | 131 | 300 | 56 | 216 | Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens] |
|
1.90e-17 | 131 | 300 | 56 | 216 | Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens] |
|
4.09e-17 | 121 | 562 | 43 | 453 | The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.18e-303 | 94 | 578 | 120 | 604 | FAD-linked oxidoreductase easE OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=easE PE=2 SV=1 |
|
1.11e-205 | 581 | 919 | 1 | 339 | 4-dimethylallyltryptophan N-methyltransferase easF OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=easF PE=2 SV=1 |
|
2.53e-204 | 581 | 919 | 1 | 339 | 4-dimethylallyltryptophan N-methyltransferase OS=Neosartorya fumigata OX=746128 GN=fgaMT PE=1 SV=1 |
|
2.11e-200 | 29 | 584 | 36 | 593 | FAD-linked oxidoreductase easE OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) OX=554155 GN=easE PE=3 SV=1 |
|
9.23e-194 | 25 | 577 | 27 | 581 | FAD-linked oxidoreductase easE OS=Trichophyton verrucosum (strain HKI 0517) OX=663202 GN=easE PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.654160 | 0.345838 |
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