Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 410688 |
Family | AA7 |
Protein Properties | Length: 415 Molecular Weight: 44419 Isoelectric Point: 6.043 |
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 | 16 | 395 | 1.10002e-42 |
SVSPVSAVTVGAGVQWEELYQAVFKQGKVIVGAGGVTVGAAGGYPQAAGHSPISPAFGLAADNVLEYEVVTAAGDLVVANGCQNEDLFWALRGGGGGTFG VVVSATHRTHPPLTNLAFAVYTINATDRSSFLDLLTNFAVIHPSLSEAGWSGYFLLSSQSLQLSRQTLLVLYILPNKDVSFAKSTLAPFLDYVEKHPKLQ GNGSVVSLSSFQEYYSQFLCGGQNSCVNSNNSAISAALSSRLIPKSLFDSRKSVEQLSDALISILERYPASILGAFVAGGAVARPREENAVNPAWRRALL LAIISSGWSDGASLEEQREVARNVSAANKLLIDLTPGSGTYINEADFNEPDWQQSFFGEHYPRLQAIKSKVDPSGLFRCH |
Full Sequence |
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Protein Sequence Length: 415 Download |
MKNMSFHDDF VAKRCSVSPV SAVTVGAGVQ WEELYQAVFK QGKVIVGAGG VTVGAAGGYP 60 QAAGHSPISP AFGLAADNVL EYEVVTAAGD LVVANGCQNE DLFWALRGGG GGTFGVVVSA 120 THRTHPPLTN LAFAVYTINA TDRSSFLDLL TNFAVIHPSL SEAGWSGYFL LSSQSLQLSR 180 QTLLVLYILP NKDVSFAKST LAPFLDYVEK HPKLQGNGSV VSLSSFQEYY SQFLCGGQNS 240 CVNSNNSAIS AALSSRLIPK SLFDSRKSVE QLSDALISIL ERYPASILGA FVAGGAVARP 300 REENAVNPAW RRALLLAIIS SGWSDGASLE EQREVARNVS AANKLLIDLT PGSGTYINEA 360 DFNEPDWQQS FFGEHYPRLQ AIKSKVDPSG LFRCHHCVGS EKWSDDLNCP RSSE* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 1.0e-5 | 23 | 393 | 388 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 7.0e-6 | 23 | 95 | 74 | + 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. | ||
pfam08031 | BBE | 1.0e-12 | 355 | 399 | 45 | + 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. |
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 | 409 | 177 | 590 | FAD binding domain-containing protein [Ajellomyces capsulatus G186AR] |
GenBank | EER27468.1 | 0 | 1 | 405 | 176 | 582 | conserved hypothetical protein [Coccidioides posadasii C735 delta SOWgp] |
GenBank | EER39924.1 | 0 | 1 | 409 | 177 | 590 | FAD binding protein [Ajellomyces capsulatus H143] |
RefSeq | XP_001541250.1 | 0 | 1 | 406 | 218 | 628 | predicted protein [Ajellomyces capsulatus NAm1] |
RefSeq | XP_002544591.1 | 0 | 1 | 409 | 173 | 582 | 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 | 3tsj_B | 0.00000000005 | 25 | 398 | 123 | 493 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 3tsj_A | 0.00000000005 | 25 | 398 | 123 | 493 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 3tsh_A | 0.00000000005 | 25 | 398 | 123 | 493 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 2bvh_D | 0.000000001 | 21 | 401 | 101 | 457 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 2bvh_C | 0.000000001 | 21 | 401 | 101 | 457 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FE499710 | 221 | 191 | 409 | 0 |
FE499710 | 221 | 191 | 409 | 0 |
FE448435 | 154 | 256 | 409 | 2.99878e-43 |
FE448435 | 154 | 256 | 409 | 2.99878e-43 |
FE499711 | 151 | 22 | 169 | 7e-39 |
Sequence Alignments (This image is cropped. Click for full image.) |
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