Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 115290 |
Family | AA7 |
Protein Properties | Length: 559 Molecular Weight: 61332.4 Isoelectric Point: 8.0055 |
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 | 115 | 341 | 0 |
PIYAVNVTRAAHVQEAVKFASRHDLRIVIRNTGHDFLGRSTAVGALSIWVHHLQKIQFHESFKCGRGSDRGYSAVTVGAGIQWEELYRQAYQRKMILAGG GCSSVGAAGGYPQGGGQSFLSPLIGLSADNVLEYEVVTADGRLVKANACQNTDLFWALRGGGGGTFGVVLSATHRTFPALHTLVFAPHNFSAPDTTTFQG LLTLFTRLNPSLSDAGWSGYFFSTSQS |
Full Sequence |
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Protein Sequence Length: 559 Download |
MIAILSIFLV VLFAPGHVHS KCIAGELCWP DAQTWASFNR SVGGRMISVA PPASPCHDPN 60 YDERACNAVR SGWNSPFWRT DQPGALQRTS WESFGEQRCL ISSNRTAACF QGAVPIYAVN 120 VTRAAHVQEA VKFASRHDLR IVIRNTGHDF LGRSTAVGAL SIWVHHLQKI QFHESFKCGR 180 GSDRGYSAVT VGAGIQWEEL YRQAYQRKMI LAGGGCSSVG AAGGYPQGGG QSFLSPLIGL 240 SADNVLEYEV VTADGRLVKA NACQNTDLFW ALRGGGGGTF GVVLSATHRT FPALHTLVFA 300 PHNFSAPDTT TFQGLLTLFT RLNPSLSDAG WSGYFFSTSQ SLTLTFLLPN RNVSYASATL 360 APLLSYAREN NIRIDGSLET YASYWDWHLQ FQCGGQESCL GLNNLGVSDV FATRLIPRSL 420 FNHEQDLLPK AMMRVMTELQ VPATYAILGG GKVREPQDSA VNPAYRDGLW LLVSPLTWRD 480 NATVAEMRAA ANLVSQANKL FIDLTPGSGT YVNEADYNEP NWQQSFFGKN YPRLYHIKRR 540 VDPINLFTCH HCVGSEFN* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 3.0e-10 | 510 | 547 | 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 | 9.0e-12 | 113 | 293 | 186 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 6.0e-17 | 115 | 261 | 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. |
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 | 3vte_A | 0.000000000000002 | 115 | 553 | 54 | 510 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0.00000000000002 | 115 | 328 | 55 | 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 | 0.00000000000002 | 115 | 328 | 55 | 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 | 0.00000000000003 | 115 | 299 | 53 | 231 | 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 | 0.00000000000003 | 115 | 299 | 53 | 231 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |