UniGene Name: sp_v3.0_unigene54526
Length: 244 nt
UniGene Fasta |
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>sp_v3.0_unigene54526
A |
Ace file of the UniGene sp_v3.0_unigene54526 |
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Annotations |
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Source | Descriptions | Term | Type | e value | Identity |
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AutoFact | Ubiquitin-conjugating enzyme E2 35 n=42 Tax=Embryophyta RepID=UBC35_ARATH | - | - | 2.0e-34 | 98% |
FL-Next | tr=Putative uncharacterized protein; Picea sitchensis (Sitka spruce) (Pinus sitchensis). | - | - | 0.0 | 98% |
Sma3 | Ubiquitin carrier protein | - | - | 0.0 | - |
Source | ECs | Term | Type | e value | Identity |
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Sma3 | Ligases, Forming carbon-nitrogen bonds, Acid--D-amino-acid ligases (peptide synthases). | EC:6.3.2.- | - | 0.0 | - |
Source | KEGGs | Term | Type | e value | Identity |
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Sma3 | Tryptophan metabolism | 00380 | 0.0 | % | |
Sma3 | Biosynthesis of siderophore group nonribosomal peptides | 01053 | 0.0 | % | |
Sma3 | Ubiquitin--protein ligase. | EC:6.3.2.19 | - | 2.094e-29 | - |
Source | Gene names |
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Sma3 | At1g16890; At1g36340; At1g64230; At1g78870; At2g16740; At3g08690; At3g08700; At4g27960; At5g25760; At5g41700; At5g50870; At5g53300; At5g56150; B0811B10.8; B1043F11.37; CHLREDRAFT_116503; CHLREDRAFT_129070; CHLREDRAFT_152525; CHLREDRAFT_160028; F17F16.19; |
Source | GOs | Term | Type | e value | Identity |
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Sma3 | nucleus | GO:0005634 | Cellular Component | 0.0 | - |
Sma3 | cytoplasm | GO:0005737 | Cellular Component | 0.0 | - |
Sma3 | vacuole | GO:0005773 | Cellular Component | 0.0 | - |
Sma3 | plasma membrane | GO:0005886 | Cellular Component | 0.0 | - |
Sma3 | UBC13-MMS2 complex | GO:0031372 | Cellular Component | 0.0 | - |
Sma3 | ubiquitin-protein ligase activity | GO:0004842 | Molecular Function | 0.0 | - |
Sma3 | protein binding | GO:0005515 | Molecular Function | 0.0 | - |
Sma3 | ATP binding | GO:0005524 | Molecular Function | 0.0 | - |
Sma3 | small conjugating protein ligase activity | GO:0019787 | Molecular Function | 0.0 | - |
Sma3 | ubiquitin-dependent protein catabolic process | GO:0006511 | Biological Process | 0.0 | - |
Sma3 | fatty acid beta-oxidation | GO:0006635 | Biological Process | 0.0 | - |
Sma3 | protein import into peroxisome matrix | GO:0016558 | Biological Process | 0.0 | - |
Sma3 | protein ubiquitination | GO:0016567 | Biological Process | 0.0 | - |
Sma3 | modification-dependent protein catabolic process | GO:0019941 | Biological Process | 0.0 | - |
Sma3 | post-translational protein modification | GO:0043687 | Biological Process | 0.0 | - |
Sma3 | cell redox homeostasis | GO:0045454 | Biological Process | 0.0 | - |
Sma3 | regulation of protein metabolic process | GO:0051246 | Biological Process | 0.0 | - |
Source | InterPros | Term | Type | e value | Identity |
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Sma3 | Ubiquitin-associated/translation elongation factor EF1B, N-terminal | IPR000449 | - | 0.0 | - |
Sma3 | Ubiquitin-conjugating enzyme, E2 | IPR000608 | - | 0.0 | - |
Sma3 | Haloacid dehalogenase-like hydrolase | IPR005834 | - | 0.0 | - |
Sma3 | HAD-superfamily hydrolase, subfamily IA, variant 3 | IPR006402 | - | 0.0 | - |
Sma3 | Thioredoxin domain | IPR013766 | - | 0.0 | - |
Sma3 | IPR015582 | - | 0.0 | - | |
Sma3 | Ubiquitin-associated/translation elongation factor EF1B, N-terminal, eukaryote | IPR015940 | - | 0.0 | - |
Sma3 | Ubiquitin-conjugating enzyme/RWD-like | IPR016135 | - | 0.0 | - |
Sma3 | IPR017936 | - | 0.0 | - | |
Sma3 | Thioredoxin, conserved site | IPR017937 | - | 0.0 | - |
Source | Species | ID | Description | e value | Identity |
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ATG | Arabidoptis thaliana | AT1G78870.1 | UBC35, UBC13A ubiquitin-conjugating enzyme 35 chr1:29650589-29652203 FORWARD LENGTH=154 | 0.0 | 97% |
RefSeq | Arabidopsis thaliana | NP_849678.1 | ubiquitin-conjugating enzyme E2 36 [Arabidopsis thaliana] | 0.0 | 98% |
RefSeq | Populus trichocarpa | XP_002330723.1 | predicted protein [Populus trichocarpa] | 0.0 | 98% |
Full-Lengther Next Prediction |
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Fln status: Internal
Fln database: coniferopsida.fasta
Fln subject: A9NUN0
Fln msg: Distance to subject end: 30 aas, your sequence is shorter than subject: 81 - 153
Fln protein:
T
Protein Length:
82
Fln nts:
A
Fln Alignment:
F51TW9002HT9X7___TQSPYEGGFVFKLELFLPEEYPMAAPKVRFLTKIYHPNIDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPN
A9NUN0_______________TQSPYEGG-VFKLELFLPEEYPMAAPKVRFLTKIYHPNIDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPN
Biología Molecular y Biotecnología de Plantas, Facultad de Ciencias y Plataforma Andaluza de Bioinformática, Universidad de Málaga, E-29071 Málaga, Spain