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CAZyme Information: PV10_08484-t45_1-p1

You are here: Home > Sequence: PV10_08484-t45_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Exophiala mesophila
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila
CAZyme ID PV10_08484-t45_1-p1
CAZy Family GT39
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
459 51510.08 5.3168
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EmesophilaCBS40295 9237 N/A 56 9181
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in PV10_08484-t45_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 23 434 1e-79 0.9759825327510917

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 3.36e-25 19 434 17 449
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 1.46e-21 34 169 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.
369658 BBE 4.37e-04 402 434 6 37
Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.
215242 PLN02441 0.006 153 193 194 233
cytokinin dehydrogenase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.44e-28 34 200 20 188
1.48e-27 34 200 48 216
3.93e-26 34 200 42 211
2.45e-25 13 198 255 440
2.45e-25 13 198 255 440

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.83e-24 6 435 22 453
The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
8.77e-24 25 198 53 227
Xylooligosaccharide oxidase from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],5L6F_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylobiose [Thermothelomyces thermophilus ATCC 42464],5L6G_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylose [Thermothelomyces thermophilus ATCC 42464]
9.43e-24 6 435 22 453
The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus]
9.43e-24 6 435 22 453
The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]
1.27e-23 6 435 22 453
The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.14e-103 2 439 7 444
FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
3.06e-100 4 440 9 443
FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
6.11e-100 4 440 9 443
FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
1.05e-97 4 441 6 445
FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
7.32e-27 14 432 58 522
FAD-linked oxidoreductase pynB OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=pynB PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000052 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in PV10_08484-t45_1-p1.