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Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 1345 |
Family | AA7 |
Protein Properties | Length: 550 Molecular Weight: 60056.1 Isoelectric Point: 6.2511 |
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 | 100 | 539 | 0 |
VDVRQADDVSKAFAFATKHHIRVIVKNTGHDYLGRSDGRGALSIWTHNLKTIDFSDNFERFQCPFDSKDGQVSAVTVGAGVQFGELYKAVAAQNKIVIAF DPPSVGAAGGYVGGGGHSVLAPTYGLPADNILEINVVTPDGSYFVANECQNKDLFWALRGGGPATFGVVLSVTYRTHPAPAAVTNVHHEVSANDSSSLRD FIAEYARLMPSIADKGYGGSFVALPNAGHLNYVLPGGNQSAAQQDWQPLVDFAASHPGLKVLQRVTMFPNFYAFFNATLCNRFKTQCTDLTGTNEILASR LLPRSLFVNSPDAIADAYMDILTRNSSNGARNFILTMSVGGGAGALGDEHSAALNPAWRKALWHTIIQAVWDDDASGDVIQHKFVDITNANQVFRDLAPE SGSYMNEADYNEPDWQTSFFGEHYERLGEIKAQVDPHDVL |
Full Sequence |
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Protein Sequence Length: 550 Download |
SHCYCLPPQR CFPSPPVWHS FSKDIGGRLI QARPAAYPCH DPHYDEAACK VAKTKWTDAL 60 WRSDQVGASQ HPQWDSFKQQ KCLINSNDTC YQGAVPIYAV DVRQADDVSK AFAFATKHHI 120 RVIVKNTGHD YLGRSDGRGA LSIWTHNLKT IDFSDNFERF QCPFDSKDGQ VSAVTVGAGV 180 QFGELYKAVA AQNKIVIAFD PPSVGAAGGY VGGGGHSVLA PTYGLPADNI LEINVVTPDG 240 SYFVANECQN KDLFWALRGG GPATFGVVLS VTYRTHPAPA AVTNVHHEVS ANDSSSLRDF 300 IAEYARLMPS IADKGYGGSF VALPNAGHLN YVLPGGNQSA AQQDWQPLVD FAASHPGLKV 360 LQRVTMFPNF YAFFNATLCN RFKTQCTDLT GTNEILASRL LPRSLFVNSP DAIADAYMDI 420 LTRNSSNGAR NFILTMSVGG GAGALGDEHS AALNPAWRKA LWHTIIQAVW DDDASGDVIQ 480 HKFVDITNAN QVFRDLAPES GSYMNEADYN EPDWQTSFFG EHYERLGEIK AQVDPHDVLA 540 CRNCVGSEAW 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 6.0e-9 | 502 | 538 | 37 | + 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. | ||
pfam01565 | FAD_binding_4 | 3.0e-13 | 96 | 241 | 148 | + 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. | ||
COG0277 | GlcD | 2.0e-16 | 105 | 539 | 445 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
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 | 0.000000000001 | 81 | 323 | 38 | 276 | A Chain A, Crystal Structure Of A Mycobacterial Protein |
PDB | 3tsj_A | 0.000000000001 | 81 | 323 | 38 | 276 | A Chain A, Crystal Structure Of A Mycobacterial Protein |
PDB | 3tsh_A | 0.000000000001 | 81 | 323 | 38 | 276 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 2bvh_D | 0.000000000006 | 104 | 279 | 47 | 206 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 2bvh_C | 0.000000000006 | 104 | 279 | 47 | 206 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
Sequence Alignments (This image is cropped. Click for full image.) |
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