UniGene Name: sp_v3.0_unigene41107
Length: 217 nt
This UniGene was originaly assembled in antisense
ACE File: antisense
Fasta: sense
UniGene Fasta (sense) |
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>sp_v3.0_unigene41107
A |
Ace file of the UniGene sp_v3.0_unigene41107 (antisense) |
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Annotations |
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Source | Descriptions | Term | Type | e value | Identity |
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AutoFact | Putative sinapyl alcohol dehydrogenase (Fragment) n=2 Tax=Pinus RepID=E5F5N9_PINAR | - | - | 2.0e-24 | 83% |
FL-Next | tr=Putative uncharacterized protein; Picea sitchensis (Sitka spruce) (Pinus sitchensis). | - | - | 0.0 | 93% |
Sma3 | Cinnamyl alcohol dehydrogenase | - | - | 2.66247e-42 | - |
Source | ECs | Term | Type | e value | Identity |
---|---|---|---|---|---|
Sma3 | Cinnamyl-alcohol dehydrogenase. | EC:1.1.1.195 | - | 5.062e-24 | - |
Source | KEGGs | Term | Type | e value | Identity |
---|---|---|---|---|---|
Sma3 | Phenylpropanoid biosynthesis | 00940 | 5.062e-24 | % | |
Sma3 | Biosynthesis of phenylpropanoids | 01061 | 5.062e-24 | % | |
Sma3 | Metabolic pathways | 01100 | 5.062e-24 | % | |
Sma3 | Biosynthesis of secondary metabolites | 01110 | 5.062e-24 | % | |
Sma3 | Mannitol dehydrogenase. | EC:1.1.1.255 | - | 0.0 | - |
Source | Gene names |
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Sma3 | AT2G21730; AT2G21890; AT4G37970; AT4G37980; AT4G39330; AT4g37970; At1g72680; At2g21730; At2g21890; At4g37970; At4g37980; At4g37990; At4g39330; AtCAD1; CAD; CAD1; CAD2; CAD3; CAD6; CAD7; CAD8; CADL1; CADL10; CADL11; CADL2; CADL3; CADL4; CADL5; CADL6; CADL7 |
Source | GOs | Term | Type | e value | Identity |
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Sma3 | cytoplasm | GO:0005737 | Cellular Component | 0.0 | - |
Sma3 | apoplast | GO:0048046 | Cellular Component | 0.0 | - |
Sma3 | protein binding | GO:0005515 | Molecular Function | 0.0 | - |
Sma3 | zinc ion binding | GO:0008270 | Molecular Function | 0.0 | - |
Sma3 | oxidoreductase activity | GO:0016491 | Molecular Function | 0.0 | - |
Sma3 | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | GO:0016616 | Molecular Function | 0.0 | - |
Sma3 | cinnamyl-alcohol dehydrogenase activity | GO:0045551 | Molecular Function | 0.0 | - |
Sma3 | mannitol dehydrogenase activity | GO:0046029 | Molecular Function | 0.0 | - |
Sma3 | cofactor binding | GO:0048037 | Molecular Function | 0.0 | - |
Sma3 | response to bacterium | GO:0009617 | Biological Process | 0.0 | - |
Sma3 | lignin biosynthetic process | GO:0009809 | Biological Process | 0.0 | - |
Sma3 | oxidation-reduction process | GO:0055114 | Biological Process | 0.0 | - |
Source | InterPros | Term | Type | e value | Identity |
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Sma3 | Alcohol dehydrogenase superfamily, zinc-type | IPR002085 | - | 0.0 | - |
Sma3 | Alcohol dehydrogenase, zinc-type, conserved site | IPR002328 | - | 0.0 | - |
Sma3 | Sugar transporter, conserved site | IPR005829 | - | 0.0 | - |
Sma3 | D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding | IPR006140 | - | 0.0 | - |
Sma3 | TonB box, conserved site | IPR010916 | - | 0.0 | - |
Sma3 | Alcohol dehydrogenase, C-terminal | IPR013149 | - | 0.0 | - |
Sma3 | Alcohol dehydrogenase GroES-like | IPR013154 | - | 0.0 | - |
Sma3 | NAD(P)-binding domain | IPR016040 | - | 0.0 | - |
Sma3 | 4Fe-4S ferredoxin, iron-sulphur binding, conserved site | IPR017900 | - | 0.0 | - |
Source | Species | ID | Description | e value | Identity |
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ATG | Arabidoptis thaliana | AT1G72680.1 | ATCAD1, CAD1 cinnamyl-alcohol dehydrogenase chr1:27359346-27360876 REVERSE LENGTH=355 | 9.0e-16 | 66% |
RefSeq | Arabidopsis thaliana | NP_177412.1 | putative cinnamyl alcohol dehydrogenase 1 [Arabidopsis thaliana] | 1.0e-15 | 66% |
RefSeq | Populus trichocarpa | XP_002322822.1 | sinapyl alcohol dehydrogenase [Populus trichocarpa] | 3.0e-18 | 66% |
Full-Lengther Next Prediction |
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Fln status: Internal
Fln database: coniferopsida.fasta
Fln subject: A9NZE7
Fln msg: Distance to subject end: 115 aas, your sequence is shorter than subject: 72 - 364
Fln protein:
Y
Protein Length:
73
Fln nts:
A
Fln Alignment:
CL8931Contig1___YFQMTEPGKSXXXXXXXXXGHMAVKFGKAFGLKVTVISTSPKKEKEAREVLGADHFLISKDEKQMLDAARSL
A9NZE7_______________YFQMTEPGKSLGVVGLGGLGHMAVKFGKAFGLKVTVISTSPQKEKEAREHLGADNFLISKDQKQMLEAARSL
Biología Molecular y Biotecnología de Plantas, Facultad de Ciencias y Plataforma Andaluza de Bioinformática, Universidad de Málaga, E-29071 Málaga, Spain