| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | Cre11.g476600.t1.2 |
| Family | AA7 |
| Protein Properties | Length: 550 Molecular Weight: 60335.1 Isoelectric Point: 6.7293 |
| Chromosome | Chromosome/Scaffold: 11 Start: 2652705 End: 2660087 |
| Description | FAD-binding Berberine family protein |
| 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 | 78 | 513 | 5.49309e-43 |
| PSSPGLIVFPMNEGDVRKVVTFAAKFRIRLVGKCSGHDQLQRSNGYGVIQLVTTKGFRNISYNETDHTITFGAGNAHKDVYAFLADRKRFAVGGTWAYVC PAGCLSNGCYGFFTKEFGSGADNVVGLRFMLFNGTTLNLDAAGPHRDLFWAILGGGASSYGVLLGITAKTYEAPDQFIIMKVFLSIWPTGLTKDQAPSVF TRFLTNLTWYQALPPHISWQLDNNPAEQRVLLQISYTGRTTVDVATEELSGLVAEWTEAGYFQEHGVEGYSDVADFAVKNSGAGPPIRRVSQSIYVDANQ DALDKVAALWETLYSDAYMSPVGSDPFDGAFNFWAQYRYGPGSYAGKAPHVARGMRTAMMEIAHENVWMRQADDSFRAAISNDVKELMEPLGNTSYQNHC STWAEYNVYVDYKTRFYQNWEGLTAVKKKYDPCNLY | |||
| Full Sequence |
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| Protein Sequence Length: 550 Download |
| MTNPARSLAL VALLAFAGFA AAEHCLPGDG TGCWPSQAEV KALVDSLSSE AEVYLPTGPN 60 ADMYMSYATD TPGNTLKPSS PGLIVFPMNE GDVRKVVTFA AKFRIRLVGK CSGHDQLQRS 120 NGYGVIQLVT TKGFRNISYN ETDHTITFGA GNAHKDVYAF LADRKRFAVG GTWAYVCPAG 180 CLSNGCYGFF TKEFGSGADN VVGLRFMLFN GTTLNLDAAG PHRDLFWAIL GGGASSYGVL 240 LGITAKTYEA PDQFIIMKVF LSIWPTGLTK DQAPSVFTRF LTNLTWYQAL PPHISWQLDN 300 NPAEQRVLLQ ISYTGRTTVD VATEELSGLV AEWTEAGYFQ EHGVEGYSDV ADFAVKNSGA 360 GPPIRRVSQS IYVDANQDAL DKVAALWETL YSDAYMSPVG SDPFDGAFNF WAQYRYGPGS 420 YAGKAPHVAR GMRTAMMEIA HENVWMRQAD DSFRAAISND VKELMEPLGN TSYQNHCSTW 480 AEYNVYVDYK TRFYQNWEGL TAVKKKYDPC NLYVVQYGPG WDLPKATCGL STTSTKRPPP 540 KRPPPRRHA* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 4.0e-13 | 65 | 512 | 478 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 2.0e-16 | 81 | 217 | 139 | + 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EDP49092.1 | 0.000000000000005 | 81 | 270 | 175 | 369 | isoamyl alcohol oxidase, putative [Aspergillus fumigatus A1163] |
| RefSeq | XP_001793119.1 | 0.000000000000002 | 92 | 254 | 37 | 205 | hypothetical protein SNOG_02515 [Phaeosphaeria nodorum SN15] |
| RefSeq | XP_001816994.1 | 0.000000000000008 | 81 | 256 | 125 | 305 | hypothetical protein [Aspergillus oryzae RIB40] |
| RefSeq | XP_002383067.1 | 0.000000000000006 | 81 | 256 | 125 | 312 | conserved hypothetical protein [Aspergillus flavus NRRL3357] |
| RefSeq | ZP_02275707.1 | 0.00000000000001 | 25 | 257 | 27 | 289 | FAD-binding protein [Francisella tularensis subsp. holarctica FSC200] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2bvh_D | 0.00000008 | 81 | 517 | 39 | 452 | B Chain B, Structural Basis For Specific Recognition Of Reelin By Its Receptors |
| PDB | 2bvh_C | 0.00000008 | 81 | 517 | 39 | 452 | B Chain B, Structural Basis For Specific Recognition Of Reelin By Its Receptors |
| PDB | 2bvh_B | 0.00000008 | 81 | 517 | 39 | 452 | B Chain B, Structural Basis For Specific Recognition Of Reelin By Its Receptors |
| PDB | 2bvh_A | 0.00000008 | 81 | 517 | 39 | 452 | B Chain B, Structural Basis For Specific Recognition Of Reelin By Its Receptors |
| PDB | 2bvg_D | 0.00000008 | 81 | 517 | 39 | 452 | B Chain B, Structural Basis For Specific Recognition Of Reelin By Its Receptors |
| Signal Peptide | ||||
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| Cleavage Site | ||||
| 22 | ||||
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| FC092815 | 263 | 171 | 433 | 0 |
| FC095564 | 80 | 456 | 535 | 0 |
| HS078295 | 223 | 83 | 299 | 0.000000000000007 |
| DY908315 | 186 | 80 | 259 | 0.00000000000004 |
| EL421203 | 194 | 81 | 259 | 0.0000000000001 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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