D
IPR035587

DUS-like, FMN-binding domain

InterPro entry
Short nameDUS-like_FMN-bd
Overlapping
homologous
superfamilies
 

Description

This entry represents a dihydrouridine synthase-like (DUS-like) FMN-binding domain
[5]
. Proteins containing this domain 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 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
[1, 2]
. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present
[5]
.

Dihydrouridine synthases (Dus) is a large family of flavoenzymes comprising eight subfamilies. They catalyse the NADPH-dependent synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Mainly, they contain two functional conserved domains, an N-terminal catalytic domain (TBD) adopting a TIM barrel fold and a unique C-terminal helical domain (HD) devoted to tRNA recognition. However, DUS2 is distinguished from its paralogues and its fungi orthologues by the acquisition of an additional domain, a double stranded RNA binding domain (dsRBD), which serves as the main tRNA binding module
[4, 3]
.

References

1.A conserved family of Saccharomyces cerevisiae synthases effects dihydrouridine modification of tRNA. Xing F, Martzen MR, Phizicky EM. RNA 8, 370-81, (2002). View articlePMID: 12003496

2.Identification of the tRNA-dihydrouridine synthase family. Bishop AC, Xu J, Johnson RC, Schimmel P, de Crecy-Lagard V. J. Biol. Chem. 277, 25090-5, (2002). View articlePMID: 11983710

3.Molecular basis for transfer RNA recognition by the double-stranded RNA-binding domain of human dihydrouridine synthase 2. Bou-Nader C, Barraud P, Pecqueur L, Perez J, Velours C, Shepard W, Fontecave M, Tisne C, Hamdane D. Nucleic Acids Res 47, 3117-3126, (2019). PMID: 30605527

4.Electrostatic Potential in the tRNA Binding Evolution of Dihydrouridine Synthases. Bou-Nader C, Bregeon D, Pecqueur L, Fontecave M, Hamdane D. Biochemistry 57, 5407-5414, (2018). PMID: 30149704

5.The 1.59 A resolution crystal structure of TM0096, a flavin mononucleotide binding protein from Thermotoga maritima. Park F, Gajiwala K, Noland B, Wu L, He D, Molinari J, Loomis K, Pagarigan B, Kearins P, Christopher J, Peat T, Badger J, Hendle J, Lin J, Buchanan S. Proteins 55, 772-4, (2004). View articlePMID: 15103641

Cross References

Contributing Member Database Entries
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.