Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 230086 |
Family | AA7 |
Protein Properties | Length: 537 Molecular Weight: 58317 Isoelectric Point: 8.8252 |
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 | 123 | 349 | 0 |
PIYTVAARKASHIQAAVGFAAARNLRLVVKNTGHDYLGRSTAAGALSIWTHQMKSMRFHHRFLPRGCSRRSKDATYLPAVTVGAGVQWEELYQAVFDRKF VIVGGGSSSVGAAGGHPQGGGHSPLSPTFGLAADNVLEFSVVTADGSLVVANRCQNQDLYWAMRGGGGGTFGIAVTATHRLYPALDSLVFAQYNLSTPDK PSFQRTLARFTELHPSLERAGWAGTFA |
Full Sequence |
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Protein Sequence Length: 537 Download |
MKTAALPLLL IVIVAFQLAQ SFRPPCQCTA FDRHCWPDSQ SWATFNASID GKLIRVVPPA 60 SPCHDPAFNR RACREARQRW SFPFWRADQP GAMQASNWES NGITDRCSID SPRNSTCSQG 120 SVPIYTVAAR KASHIQAAVG FAAARNLRLV VKNTGHDYLG RSTAAGALSI WTHQMKSMRF 180 HHRFLPRGCS RRSKDATYLP AVTVGAGVQW EELYQAVFDR KFVIVGGGSS SVGAAGGHPQ 240 GGGHSPLSPT FGLAADNVLE FSVVTADGSL VVANRCQNQD LYWAMRGGGG GTFGIAVTAT 300 HRLYPALDSL VFAQYNLSTP DKPSFQRTLA RFTELHPSLE RAGWAGTFAI TNTTGLTLSC 360 RDVDTANTGI ATAGIPLLLA SRLIPRTTVA YSPGNLAEVM VRIRELFPRV SLTGVFVGGG 420 AVSRDDRDNA VNPAWRRALW HVILGRSWSD GDDRAEQRAR AELSAANAML IDLTPGSGAY 480 GNEADFSEPQ WQESLFGEHY TRLLAIKKRV DPAGIFRCHH CVGSEEWSED LLCATR* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 4.0e-9 | 479 | 523 | 45 | + 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-12 | 127 | 517 | 441 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 1.0e-12 | 123 | 274 | 153 | + 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 - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 4dns_B | 0.0000000002 | 123 | 306 | 55 | 227 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 4dns_A | 0.0000000002 | 123 | 306 | 55 | 227 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3tsj_B | 0.0000000004 | 123 | 306 | 53 | 225 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3tsj_A | 0.0000000004 | 123 | 306 | 53 | 225 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3tsh_A | 0.0000000004 | 123 | 306 | 53 | 225 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |