A0A2V1A6R9 · A0A2V1A6R9_9ASCO
- ProteintRNA-dihydrouridine(47) synthase [NAD(P)(+)]
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids602 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs. Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation.
Catalytic activity
- 5,6-dihydrouridine47 in tRNA + NAD+ = uridine47 in tRNA + NADH + H+This reaction proceeds in the backward direction.
- a 5,6-dihydrouridine in mRNA + NAD+ = a uridine in mRNA + NADH + H+This reaction proceeds in the backward direction.
- a 5,6-dihydrouridine in mRNA + NADP+ = a uridine in mRNA + NADPH + H+This reaction proceeds in the backward direction.
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA dihydrouridine synthase activity | |
Molecular Function | RNA binding | |
Molecular Function | tRNA-dihydrouridine47 synthase activity | |
Biological Process | mRNA processing |
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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Metschnikowiaceae > Metschnikowiaceae incertae sedis > Candida/Metschnikowiaceae
Accessions
- Primary accessionA0A2V1A6R9
Proteomes
Organism-specific databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-28 | Basic and acidic residues | ||||
Sequence: MTEDDKRDIDASTEPVAKKARTDNYDKG | ||||||
Region | 1-90 | Disordered | ||||
Sequence: MTEDDKRDIDASTEPVAKKARTDNYDKGLAPIKPEFVVESVKVEEAYDDEEAEGGDRGQQEGSKRSKKKRGQNKKRDLKQQKEDVRLCSS | ||||||
Domain | 82-114 | C3H1-type | ||||
Sequence: KEDVRLCSSLVDPSDPKECKFGPDKCRNTHDVT | ||||||
Zinc finger | 82-114 | C3H1-type | ||||
Sequence: KEDVRLCSSLVDPSDPKECKFGPDKCRNTHDVT |
Sequence similarities
Belongs to the dus family. Dus3 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length602
- Mass (Da)68,423
- Last updated2018-09-12 v1
- ChecksumD6AD94D8E06DD0DE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-28 | Basic and acidic residues | ||||
Sequence: MTEDDKRDIDASTEPVAKKARTDNYDKG |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PKFP01000001 EMBL· GenBank· DDBJ | PVH13780.1 EMBL· GenBank· DDBJ | Genomic DNA |