SustainPineDB

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Assembly info
Unigenes
SNPs
SSRs
Descriptions
GOs
ECs
KEGGs
InterPros
miRNAs

Assembly Name: SustainPine v3.0

UniGene Name: sp_v3.0_unigene106134

Length: 186 nt

UniGene Fasta

>sp_v3.0_unigene106134
TGGAAATCCAAGAAGGGAAAGGTGGTGTGAAGGTGTGCGTTACAGGAGCAGGGGGGTACATTGGATCATGGCTCGTCAAGAATCTTCTCCAAAGAGGCTACACCGTCAACGCCACTCTCAGAGATCCACGTACTATTTCCTTTACATTCGTCTCAAGCGTAAATTTTAATGCTAGTTCTGGTTAGA

Ace file of the UniGene sp_v3.0_unigene106134

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Annotations

Source	Descriptions	Term	Type	e value	Identity
AutoFact	Cinnamoyl-CoA reductase, putative n=1 Tax=Ricinus communis RepID=B9RVL9_RICCO	-	-	3.0e-08	73%
FL-Next	tr=Putative uncharacterized protein; Picea sitchensis (Sitka spruce) (Pinus sitchensis).	-	-	0.0	86%
Sma3	Dihydroflavonol 4-reductase	-	-	0.0	-

Source	ECs	Term	Type	e value	Identity
Sma3	Dihydrokaempferol 4-reductase.	EC:1.1.1.219	-	1.275e-32	-

Source	KEGGs	Term	Type	e value	Identity
Sma3	Flavonoid biosynthesis	00941		1.275e-32	%
Sma3	Biosynthesis of phenylpropanoids	01061		1.275e-32	%
Sma3	Metabolic pathways	01100		1.275e-32	%
Sma3	Biosynthesis of secondary metabolites	01110		1.275e-32	%
Sma3	Cinnamoyl-CoA reductase.	EC:1.2.1.44	-	1.654e-12	-

Source	KEGGs	Term	e value	Identity
Sma3	Phenylpropanoid biosynthesis	00940	1.654e-12	%
Sma3	Biosynthesis of phenylpropanoids	01061	1.654e-12	%
Sma3	Metabolic pathways	01100	1.654e-12	%
Sma3	Biosynthesis of secondary metabolites	01110	1.654e-12	%

Source	Gene names
Sma3	A; ADH; AN6; AT1G15950; AT4g27250; ApDFR; At1g09490; At1g09500; At1g15950; At1g76470; At1g80820; At4g27250; CAD; CAD1; CAD1-1; CAD1-7; CCR; CCR1; CCRL3; CCRL4; CCRL5; CtDFR; DFR; DFR-A; DFR-B; DFR-BN-1; DFR-BO-1; DFR-C; DFR-FL2; DFR1; DFR2; DFR5; DFRA; Df

Source	GOs	Term	Type	Identity
Sma3	plasma membrane	GO:0005886	Cellular Component	-
Sma3	catalytic activity	GO:0003824	Molecular Function	-
Sma3	3-beta-hydroxy-delta5-steroid dehydrogenase activity	GO:0003854	Molecular Function	-
Sma3	binding	GO:0005488	Molecular Function	-
Sma3	transcription repressor activity	GO:0016564	Molecular Function	-
Sma3	cinnamoyl-CoA reductase activity	GO:0016621	Molecular Function	-
Sma3	dihydrokaempferol 4-reductase activity	GO:0045552	Molecular Function	-
Sma3	coenzyme binding	GO:0050662	Molecular Function	-
Sma3	steroid biosynthetic process	GO:0006694	Biological Process	-
Sma3	regulation of nitrogen utilization	GO:0006808	Biological Process	-
Sma3	flavonoid biosynthetic process	GO:0009813	Biological Process	-
Sma3	cellular metabolic process	GO:0044237	Biological Process	-
Sma3	oxidation-reduction process	GO:0055114	Biological Process	-

Source	InterPros	Term	Type	Identity
Sma3	Bacterial transferase hexapeptide repeat	IPR001451	-	-
Sma3	NAD-dependent epimerase/dehydratase	IPR001509	-	-
Sma3	3-beta hydroxysteroid dehydrogenase/isomerase	IPR002225	-	-
Sma3	eIF4-gamma/eIF5/eIF2-epsilon	IPR003307	-	-
Sma3	NmrA-like	IPR008030	-	-
Sma3	NAD(P)-binding domain	IPR016040	-	-

Source	Species	ID	Description	e value	Identity
ATG	Arabidoptis thaliana	AT1G09490.1	NAD(P)-binding Rossmann-fold superfamily protein chr1:3064172-3065815 FORWARD LENGTH=322	6.0e-13	75%
RefSeq	Arabidopsis thaliana	NP_172420.1	Rossmann-fold NAD(P)-binding domain-containing protein [Arabidopsis thaliana]	7.0e-13	75%
RefSeq	Populus trichocarpa	XP_002319268.1	predicted protein [Populus trichocarpa]	1.0e-11	90%

Full-Lengther Next Prediction

Fln status: Putative N-terminus

Fln database: coniferopsida.fasta

Fln subject: A9P186

Fln msg: Unexpected STOP codon at 3' end. Distance to subject end: 165 aas, atg_distance in limit (1-15): atg_distance = 2, W2: There is no M at the beginning, your sequence is shorter than subject: 61 - 227

Fln protein: EIQEGKGGVKVCVTGAGGYIGSWLVKNLLQRGYTVNATLRDPRTISFTFVSSVNFNASSG*

Protein Length: 62

Fln nts: TGGAAATCCAAGAAGGGAAAGGTGGTGTGAAGGTGTGCGTTACAGGAGCAGGGGGGTACATTGGATCATGGCTCGTCAAGAATCTTCTCCAAAGAGGCTACACCGTCAACGCCACTCTCAGAGATCCACGTACTATTTCCTTTACATTCGTCTCAAGCGTAAATTTTAATGCTAGTTCTGGTTAGA

Fln Alignment:

AllPine_a_c37860___EIQEGKGGVKVCVTGAGGYIGSWLVKNLLQRGYTVNATLRDPR
A9P186________________QIQEAKAGVKMCVTGAGGYIGSWLVKNLLQRGYAVNATLRDPQ

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Biología Molecular y Biotecnología de Plantas, Facultad de Ciencias y Plataforma Andaluza de Bioinformática, Universidad de Málaga, E-29071 Málaga, Spain