Q06053 · DUS3_YEAST
- ProteintRNA-dihydrouridine(47) synthase [NAD(P)(+)]
- GeneDUS3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids668 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs (PubMed:12003496, PubMed:14970222).
Specifically modifies U47 in cytoplasmic tRNAs (PubMed:14970222).
Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation (By similarity).
Specifically modifies U47 in cytoplasmic tRNAs (PubMed:14970222).
Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation (By similarity).
Catalytic activity
- 5,6-dihydrouridine47 in tRNA + NAD+ = H+ + NADH + uridine47 in tRNAThis reaction proceeds in the backward direction.
- a 5,6-dihydrouridine in mRNA + NAD+ = a uridine in mRNA + H+ + NADHThis reaction proceeds in the backward direction.
- a 5,6-dihydrouridine in mRNA + NADP+ = a uridine in mRNA + H+ + NADPHThis reaction proceeds in the backward direction.
Cofactor
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 299-301 | FMN (UniProtKB | ChEBI) | ||||
Sequence: PLT | ||||||
Binding site | 354 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 386 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 426 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 457 | FMN (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 509-511 | FMN (UniProtKB | ChEBI) | ||||
Sequence: NGD | ||||||
Binding site | 534-535 | FMN (UniProtKB | ChEBI) | ||||
Sequence: AR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nuclear periphery | |
Cellular Component | nucleus | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA binding | |
Molecular Function | mRNA dihydrouridine synthase activity | |
Molecular Function | tRNA dihydrouridine synthase activity | |
Molecular Function | tRNA-dihydrouridine47 synthase activity | |
Biological Process | mRNA processing | |
Biological Process | tRNA modification |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nametRNA-dihydrouridine(47) synthase [NAD(P)(+)]
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ06053
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000162155 | 1-668 | tRNA-dihydrouridine47 synthase [NAD(P)+] | |||
Sequence: MEQNAEKRSIVGDDNSTVKRQDTSPSKGIAHIKPEYIVPLKQNENQKVAIYDEEMSSDRMTNEFAGGTNKKNKNGRGKKRGQNKNRDNRQVKEQNVLCPRLIHGDISKCSFGDNCRFVHDINLYLSTKKPEVESNIFPSCPVFNSLGFCPMGFKCRFLSSHLNKEDNILISKKEIDPDAQTIWSVKGEVNHISPERKLDLIKRRFPFTKSNEILEIIDSFQQECRDSMKPEEEVESTPQLKKQDPDVEQPVAPQVEQRNKELSEHRMKQREVYLKYKDTRYFAQEKKPLDLYHKKIVSPLTTVGNLPYRRLMRKLGADVTYSEMALAVPLIQGTNSEWALPKAHTSEFPGFGVQVACSKAWQAAKAAEALANSVSEISEINLNSGCPIDLLYRQGSGSALLDNPARMIRCLNAMNYVSKDIPITVKIRTGTKEGHPIAEGLVKRLVNETDVAAITLHGRSRQQRYTKSADWDYVSQVADTLRSAEADFIETEQGKEGRDSKNRIQFVGNGDVNNFEDWYRYLNGNENIDSVMVARGALIKPWIFEEVESQQYLDKTSTERLDILRDYAQFSMEHWGTDEYGISQCRRFFCEFMSFFHRYVPMGICERYPVKLNERPPNWCGRDELETLMGSTDVNDWIKLSDLFFGKTDENFVFVPKHKSSSYANRDS |
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MEQNAEKRSIVGDDN | ||||||
Region | 1-31 | Disordered | ||||
Sequence: MEQNAEKRSIVGDDNSTVKRQDTSPSKGIAH | ||||||
Region | 59-92 | Disordered | ||||
Sequence: RMTNEFAGGTNKKNKNGRGKKRGQNKNRDNRQVK | ||||||
Zinc finger | 92-122 | C3H1-type 1 | ||||
Sequence: KEQNVLCPRLIHGDISKCSFGDNCRFVHDIN | ||||||
Zinc finger | 134-164 | C3H1-type 2 | ||||
Sequence: SNIFPSCPVFNSLGFCPMGFKCRFLSSHLNK | ||||||
Compositional bias | 227-242 | Basic and acidic residues | ||||
Sequence: SMKPEEEVESTPQLKK | ||||||
Region | 227-264 | Disordered | ||||
Sequence: SMKPEEEVESTPQLKKQDPDVEQPVAPQVEQRNKELSE |
Sequence similarities
Belongs to the Dus family. Dus3 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length668
- Mass (Da)76,596
- Last updated2008-04-29 v2
- Checksum0DA116A41699E9C9
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MEQNAEKRSIVGDDN | ||||||
Compositional bias | 227-242 | Basic and acidic residues | ||||
Sequence: SMKPEEEVESTPQLKK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U19729 EMBL· GenBank· DDBJ | AAB82358.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
Z18944 EMBL· GenBank· DDBJ | CAA79376.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
BK006945 EMBL· GenBank· DDBJ | DAA09701.1 EMBL· GenBank· DDBJ | Genomic DNA |