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Links from Protein

Items: 5

1.

tRNA-dihydrouridine synthase

Members of this family catalyse 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 archae. 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. Dus 1 (Swiss:Q9HGN6) from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 (Swiss:P53720) acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD [1]. Some family members may be targeted to the mitochondria and even have a role in mitochondria [1]. [1]. 12003496. A conserved family of Saccharomyces cerevisiae synthases effects dihydrouridine modification of tRNA. Xing F, Martzen MR, Phizicky EM;. RNA 2002;8:370-381. (from Pfam)

GO Terms:
Biological Process:
tRNA processing (GO:0008033)
Molecular Function:
tRNA dihydrouridine synthase activity (GO:0017150)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2024-10-16
Family Accession:
NF013380.5
Method:
HMM
2.
new record, indexing in progress
Family Accession:
3.
new record, indexing in progress
Family Accession:
4.

tRNA dihydrouridine(16) synthase DusC

Gene:
dusC
GO Terms:
Biological Process:
tRNA dihydrouridine synthesis (GO:0002943)
Molecular Function:
tRNA dihydrouridine synthase activity (GO:0017150)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2021-08-26
Family Accession:
NF007838.0
Method:
HMM
5.

tRNA dihydrouridine(16) synthase DusC

tRNA dihydrouridine(16) synthase DusC catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines

Date:
2019-06-19
Family Accession:
10793415
Method:
Sparcle
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