Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 77373 |
Family | AA7 |
Protein Properties | Length: 574 Molecular Weight: 62906.2 Isoelectric Point: 7.5555 |
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 | 38 | 181 | 3e-21 |
WPDRSTCKAAQVFYPASEQQIVDAVAFGVRNNMKMKVVTRLSHSIPKLVCPGGDQGLVISTKNYSRGIVIDRAAMTVTVDSGVELRNFVDTLASSQLAFP QSSYWSGVTIGGLLSTGAHGSSLRDLGSAVHEYVTSIRLVVPAS |
Full Sequence |
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Protein Sequence Length: 574 Download |
MLTLSIVFFA DVLALPPPAV TCRSGNSNCT ISGTYGTWPD RSTCKAAQVF YPASEQQIVD 60 AVAFGVRNNM KMKVVTRLSH SIPKLVCPGG DQGLVISTKN YSRGIVIDRA AMTVTVDSGV 120 ELRNFVDTLA SSQLAFPQSS YWSGVTIGGL LSTGAHGSSL RDLGSAVHEY VTSIRLVVPA 180 SPAEGYAKVL TFTQASEDLD AVKVSLGVLG VLSKITLKVE PMFKRSVTNT MRSDSDLEDQ 240 VATFANGNDY GDITWYPSMN QAVYRIDQRV PSIVPGNGVN DFIGFQPTAV LISQATRTTE 300 RVFEFTRDTQ GTCNRARLQA FTLWTTGYGL KNNGVLFTGY PLIGNQNRIQ TSGTCYNSSS 360 SLFTCPWDPS IDGLFFHQTT ISIALERSRD FILDVKRLRN ATLNGLCGPD GYSGSLMRYV 420 KKSSAYLGKP EDSVDIDVTY YRADDANTPR LNEDVLEELE QMAVFKYQGT PHWGKNRNVA 480 FVNASRKYPN LPKFLDAKKR LDPNGLFSSE WSDLVLGVTT AGLTSDKDHC ALEGLCICSS 540 DRHCAPERGY FCRPGRVFQQ ARVCRFEELL SVE* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01565 | FAD_binding_4 | 3.0e-15 | 46 | 177 | 134 | + 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 | 3.0e-18 | 46 | 292 | 250 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
PLN00107 | PLN00107 | 6.0e-102 | 328 | 565 | 245 | + FAD-dependent oxidoreductase; Provisional | ||
TIGR01677 | pln_FAD_oxido | 0 | 16 | 565 | 557 | + plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | NP_001152512.1 | 0 | 16 | 564 | 45 | 609 | FAD binding domain containing protein [Zea mays] |
RefSeq | XP_002267268.1 | 0 | 16 | 564 | 7 | 556 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002466918.1 | 0 | 16 | 564 | 55 | 621 | hypothetical protein SORBIDRAFT_01g016650 [Sorghum bicolor] |
RefSeq | XP_002520499.1 | 0 | 12 | 564 | 20 | 574 | d-lactate dehydrogenase, putative [Ricinus communis] |
RefSeq | XP_002529978.1 | 0 | 16 | 564 | 25 | 581 | gulonolactone oxidase, putative [Ricinus communis] |
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 | 2vfv_A | 0.000000003 | 34 | 224 | 9 | 185 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 2vfu_A | 0.000000003 | 34 | 224 | 9 | 185 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 2vft_A | 0.000000003 | 34 | 224 | 9 | 185 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |