y
Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 230122 |
Family | AA7 |
Protein Properties | Length: 560 Molecular Weight: 60893.8 Isoelectric Point: 8.7469 |
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 | 357 | 0 |
PIYAVAARKASHIQAAVGFAAARNLRLVVKNTGHDYLGRSTAAGALSIWTHQMKSMRFHHRFLPRGCSRRSKDATYLPAVTVGAGVQWEELYQAVFDRKF VIVGGGSSSVGAAGGHPQGGGHSPLSPTFGLTADNVLEFSVVTADGSLVVANRCQNQDLYWAMRGGGGGTFGIAVTATHRLYPALDSLVFAQYNLSTPDK PSFQRTLARFTELHPSLERAGWAGTFAITNTTGLT |
Full Sequence |
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Protein Sequence Length: 560 Download |
MKTATVPLLL IVIVAFHLAQ SFRPPCQCTA FDRHCWPDSQ SWATFNASID GKLIRVVPPA 60 SPCHDPAFNR RACREARQRW SFPFWRADQP GAMQASNWES NGITDRCLID SPRNSSCSQG 120 SVPIYAVAAR KASHIQAAVG FAAARNLRLV VKNTGHDYLG RSTAAGALSI WTHQMKSMRF 180 HHRFLPRGCS RRSKDATYLP AVTVGAGVQW EELYQAVFDR KFVIVGGGSS SVGAAGGHPQ 240 GGGHSPLSPT FGLTADNVLE FSVVTADGSL VVANRCQNQD LYWAMRGGGG GTFGIAVTAT 300 HRLYPALDSL VFAQYNLSTP DKPSFQRTLA RFTELHPSLE RAGWAGTFAI TNTTGLTLSG 360 SLQSFPSFQE FRLAIQCQGR SSCRDVDTAN TGIATAGIPL LLASRLIPRT TVAYSPGNLA 420 EVMVRIRELF PRVSLTGVFV GGGAVSRDDR DNAVNPAWRR ALWHVILGSS WSDGDDRAEQ 480 RARAELSAAN AMLIDLTPGS GAYGNEADFN EPQWQESLFG EHYTRLLAIK KRVDPAGIFR 540 CYHCVGSEEW SEDLLCATR* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 5.0e-9 | 502 | 540 | 39 | + 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 | 1.0e-12 | 122 | 540 | 444 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 7.0e-13 | 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 - 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 | 26 | 556 | 28 | 590 | FAD binding domain-containing protein [Ajellomyces capsulatus G186AR] |
GenBank | EER27468.1 | 0 | 23 | 559 | 24 | 589 | conserved hypothetical protein [Coccidioides posadasii C735 delta SOWgp] |
RefSeq | XP_001261609.1 | 0 | 26 | 556 | 23 | 584 | FAD binding domain protein [Neosartorya fischeri NRRL 181] |
RefSeq | XP_001263995.1 | 0 | 30 | 548 | 30 | 560 | FAD binding domain protein [Neosartorya fischeri NRRL 181] |
RefSeq | XP_753129.2 | 0 | 11 | 548 | 14 | 560 | FAD/FMN-containing protein [Aspergillus fumigatus Af293] |
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 | 0.0000000006 | 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 | 0.0000000006 | 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 | 0.0000000009 | 113 | 306 | 41 | 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 | 0.0000000009 | 113 | 306 | 41 | 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 | 0.0000000009 | 113 | 306 | 41 | 225 | 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 | ||||
21 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EH092233 | 234 | 35 | 268 | 0 |
EH092089 | 218 | 135 | 351 | 0 |
FE448436 | 254 | 119 | 348 | 0 |
FP063932 | 204 | 26 | 224 | 0 |
FE499711 | 246 | 127 | 348 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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