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CAZyme Information: CPSG_00803-t26_1-p1
You are here: Home > Sequence: CPSG_00803-t26_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 | Coccidioides posadasii | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides posadasii | |||||||||||
| CAZyme ID | CPSG_00803-t26_1-p1 | |||||||||||
| CAZy Family | AA4 | |||||||||||
| CAZyme Description | conserved hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| AA7 | 129 | 570 | 6.1e-57 | 0.9454148471615721 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 396238 | FAD_binding_4 | 2.48e-18 | 128 | 272 | 5 | 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 | 1.69e-11 | 532 | 569 | 1 | 38 | 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. |
| 223354 | GlcD | 1.67e-10 | 118 | 569 | 23 | 450 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 1.05e-59 | 20 | 581 | 496 | 1055 | |
| 1.05e-59 | 20 | 581 | 496 | 1055 | |
| 3.66e-16 | 135 | 577 | 81 | 497 | |
| 2.03e-15 | 132 | 569 | 172 | 586 | |
| 1.08e-14 | 130 | 575 | 68 | 489 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5.99e-88 | 27 | 588 | 28 | 574 | 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] |
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| 3.88e-75 | 5 | 587 | 3 | 597 | 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] |
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| 7.04e-17 | 125 | 569 | 32 | 491 | Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_A Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6] |
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| 3.32e-16 | 101 | 295 | 24 | 202 | The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus] |
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| 7.82e-16 | 101 | 295 | 24 | 202 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 9.23e-240 | 1 | 588 | 1 | 588 | Uncharacterized FAD-linked oxidoreductase ARB_02478 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07056 PE=1 SV=2 |
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| 1.44e-138 | 26 | 589 | 30 | 590 | FAD-linked oxidoreductase notD OS=Aspergillus sp. (strain MF297-2) OX=877550 GN=notD PE=1 SV=1 |
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| 3.63e-137 | 27 | 586 | 25 | 576 | FAD-linked oxidoreductase malF OS=Malbranchea aurantiaca OX=78605 GN=malF PE=1 SV=1 |
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| 5.52e-128 | 3 | 586 | 6 | 581 | FAD-linked oxidoreductase easE OS=Epichloe festucae var. lolii OX=73839 GN=easE PE=2 SV=1 |
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| 9.32e-125 | 17 | 589 | 17 | 582 | FAD-linked oxidoreductase notD' OS=Aspergillus versicolor OX=46472 GN=notD' PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.000225 | 0.999734 | CS pos: 20-21. Pr: 0.9781 |