http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID239200
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present. |
| title | DUS_like_FMN |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8466052 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8484452 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
| Predicate | Subject |
|---|---|
| has component | http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9NX74 http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9D7B1 |
Total number of triples: 7.