Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 98904 |
Family | AA7 |
Protein Properties | Length: 569 Molecular Weight: 61234.3 Isoelectric Point: 6.7705 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 113 | 310 | 0 |
PMYVVDVSTVSQVQKAVSFASQHNLRLVIKNSGHDMTGKNTAPGSLSIWVHHLKDITFSDKSHGLAEYENTPSVKVGAGVQWEEVYTAAHKNKRTVVGAQ CVSVGAAGGYPQGGGHSQLSPSFGLAADNVLEYDVVTADGKLVVANSCQNKELFWALRGGGGGTFGVVTAVTYVAHPALTNLVFASYIITTGPNSTSS |
Full Sequence |
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Protein Sequence Length: 569 Download |
MITFLPLSLR GAAAAGSCRC LPSQECWPDA KTWESFNASV GGALIAAKPL GFPCHDPYFD 60 ENACKLVTEN SGDPFWRSDQ PSALQVPNME MDGDKGCLLR GDRASECLQG AVPMYVVDVS 120 TVSQVQKAVS FASQHNLRLV IKNSGHDMTG KNTAPGSLSI WVHHLKDITF SDKSHGLAEY 180 ENTPSVKVGA GVQWEEVYTA AHKNKRTVVG AQCVSVGAAG GYPQGGGHSQ LSPSFGLAAD 240 NVLEYDVVTA DGKLVVANSC QNKELFWALR GGGGGTFGVV TAVTYVAHPA LTNLVFASYI 300 ITTGPNSTSS AFKDLLAKVI SLNPSMADAG WGGFFIAAGK TLIAQYLLPN KDMAFAEKSL 360 QPLLAYVEGW KNELVVVSGK IKEFSSYYEW HLENQCTNGK CGFPSGFSQF EASRLIPRTL 420 AEKSPYKLAE ALVSLGEMGF QRISGYLVGG GKVSKAQDNA VNPAWRNALL HVLYVRPFAE 480 NSTMETKSSM ASEMSSGYKM LTDLTPGSGS YMNEANRNEP SWQQSFFGSN YDALKKIKDK 540 VDPSGLFVCY HCVGSEDWSP DLNCRVSR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 3.0e-8 | 510 | 547 | 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. | ||
COG0277 | GlcD | 9.0e-11 | 111 | 547 | 455 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 9.0e-17 | 113 | 258 | 147 | + 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 oxidises 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. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | EEH07998.1 | 0 | 5 | 567 | 16 | 593 | FAD binding domain-containing protein [Ajellomyces capsulatus G186AR] |
GenBank | EER27468.1 | 0 | 2 | 566 | 7 | 588 | conserved hypothetical protein [Coccidioides posadasii C735 delta SOWgp] |
GenBank | EER39924.1 | 0 | 5 | 567 | 16 | 593 | FAD binding protein [Ajellomyces capsulatus H143] |
RefSeq | XP_002150632.1 | 0 | 15 | 566 | 30 | 569 | isoamyl alcohol oxidase, putative [Penicillium marneffei ATCC 18224] |
RefSeq | XP_002544591.1 | 0 | 18 | 566 | 24 | 584 | predicted protein [Uncinocarpus reesii 1704] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3tsj_B | 3e-16 | 96 | 547 | 37 | 487 | A Chain A, Pectin Methylesterase From Yersinia Enterocolitica |
PDB | 3tsj_A | 3e-16 | 96 | 547 | 37 | 487 | A Chain A, Pectin Methylesterase From Yersinia Enterocolitica |
PDB | 3tsh_A | 3e-16 | 96 | 547 | 37 | 487 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 2bvh_D | 0.00000000001 | 113 | 336 | 39 | 247 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 2bvh_C | 0.00000000001 | 113 | 336 | 39 | 247 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
Signal Peptide | ||||
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Cleavage Site | ||||
15 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FE499710 | 220 | 350 | 569 | 0 |
FE448436 | 264 | 109 | 347 | 0 |
FE499711 | 256 | 117 | 347 | 0 |
FE448435 | 183 | 387 | 569 | 0 |
EH092233 | 232 | 23 | 253 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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