y
Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 1054 |
Family | AA7 |
Protein Properties | Length: 547 Molecular Weight: 59734.6 Isoelectric Point: 7.9086 |
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 | 109 | 284 | 1.4013e-45 |
SSVSHIQAGVVFAKKYNLRLAIKSSGHDWLGRSTAPGSLCIWLHHLTNIFTNDSFVPQSCPVSDPVPAVTAQPGVTWDFLYDFLRQRNRVAVGPMGSSPS AAGGFVQGGGHGPLSRTFGYAADNALEFTVVTADGRVRVANRCRNPDLFWALKGGGGGTFGVVVSATYRTFPDLQL |
Full Sequence |
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Protein Sequence Length: 547 Download |
ESSCKCTPRS SCWPSSTIWS AFNRSIDGRL LAPKPYAWPC HTPQYDPVAC SAARQLQNNP 60 FARSEVVGAM QYPNWESGIT GFGCPLNGSG ALSSPCYQDD VSIYAINVSS VSHIQAGVVF 120 AKKYNLRLAI KSSGHDWLGR STAPGSLCIW LHHLTNIFTN DSFVPQSCPV SDPVPAVTAQ 180 PGVTWDFLYD FLRQRNRVAV GPMGSSPSAA GGFVQGGGHG PLSRTFGYAA DNALEFTVVT 240 ADGRVRVANR CRNPDLFWAL KGGGGGTFGV VVSATYRTFP DLQLGYVQTL FIAASATRSS 300 HEDLIAKFVE VTPSMDEARL AGYFFLYTNY ITLSFVLPNG TAAEARAAFA PLVSYVEGHP 360 QLFVITYTVT SYPNFVQWHD GVLCATNPGV CTDLTGAPRA LATRFMPRAI IQDSPAVLTN 420 ALVRILFERN FSPIFGLFVF GGAAASVRGR NNSLSAVWRE ALWHVSLSRT WNDSTTVKER 480 QQIFQYLTTT DDILRNITPG GGCYKNEADY FEPYWQDAFF GEKYSALKAI KESVDPTGLF 540 LCWKCVG 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 1.0e-5 | 503 | 540 | 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 | 1.0e-8 | 109 | 540 | 459 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 7.0e-13 | 108 | 249 | 143 | + 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 | 1 | 547 | 25 | 580 | FAD binding domain-containing protein [Ajellomyces capsulatus G186AR] |
GenBank | EER39924.1 | 0 | 1 | 547 | 25 | 580 | FAD binding protein [Ajellomyces capsulatus H143] |
RefSeq | XP_001263995.1 | 0 | 5 | 547 | 28 | 558 | FAD binding domain protein [Neosartorya fischeri NRRL 181] |
RefSeq | XP_001541250.1 | 0 | 3 | 547 | 68 | 621 | predicted protein [Ajellomyces capsulatus NAm1] |
RefSeq | XP_002544591.1 | 0 | 4 | 547 | 24 | 572 | 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 | 3rja_A | 0.000000000000002 | 76 | 540 | 4 | 463 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 3rj8_A | 0.000000000000002 | 76 | 540 | 4 | 463 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
PDB | 4dns_B | 0.000000000002 | 103 | 317 | 56 | 260 | 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 | 0.000000000002 | 103 | 317 | 56 | 260 | 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 | 0.000000000002 | 99 | 315 | 49 | 256 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FE469704 | 255 | 185 | 439 | 0 |
FE469703 | 124 | 5 | 128 | 0 |
FE469703 | 68 | 133 | 200 | 0 |
FE449605 | 171 | 133 | 303 | 0 |
FE449605 | 56 | 73 | 128 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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