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Search results 101 to 122 out of 122 for Dus2

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Type Details Score
Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Protein Domain
IPR044463 | DUS2_DSRM
Type: Domain
Description: 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 [, ]. This entry represents the double stranded RNA binding domain of DUS2 [].
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Publication
30149704 | -
First Author: Bou-Nader C
Year: 2018
Journal: Biochemistry
Title: Electrostatic Potential in the tRNA Binding Evolution of Dihydrouridine Synthases.
Volume: 57
Issue: 37
Pages: 5407-5414
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Publication
30605527 | -
First Author: Bou-Nader C
Year: 2019
Journal: Nucleic Acids Res
Title: Molecular basis for transfer RNA recognition by the double-stranded RNA-binding domain of human dihydrouridine synthase 2.
Volume: 47
Issue: 6
Pages: 3117-3126
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Protein
Q9D7B1
Organism: Mus musculus/domesticus
Length: 493  
Fragment?: false
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Protein
Q14A90
Organism: Mus musculus/domesticus
Length: 493  
Fragment?: false
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Publication
15103641 | -
First Author: Park F
Year: 2004
Journal: Proteins
Title: The 1.59 A resolution crystal structure of TM0096, a flavin mononucleotide binding protein from Thermotoga maritima.
Volume: 55
Issue: 3
Pages: 772-4
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Protein Domain
IPR001269 | DUS_fam
Type: Family
Description: 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 [, ]. Dus 1 () from Saccharomyces cerevisiae (Baker's yeast) acts on pre-tRNA-Phe, while Dus 2 () 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 []. Some family members may be targeted to the mitochondria and even have a role in mitochondria []. DUS3 (not included in this entry) contains an extra zinc finger N-terminal to the Dus domain.
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Protein Domain
IPR035587 | DUS-like_FMN-bd
Type: Domain
Description: This entry represents a dihydrouridine synthase-like (DUS-like) FMN-binding domain []. 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 [, ]. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present [].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 [, ].
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Protein
Q32M08
Organism: Mus musculus/domesticus
Length: 324  
Fragment?: false
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Protein
A0A0R4J016
Organism: Mus musculus/domesticus
Length: 324  
Fragment?: false
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Publication
12003496 | -
First Author: Xing F
Year: 2002
Journal: RNA
Title: A conserved family of Saccharomyces cerevisiae synthases effects dihydrouridine modification of tRNA.
Volume: 8
Issue: 3
Pages: 370-81
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Protein
A4FTV5
Organism: Mus musculus/domesticus
Length: 274  
Fragment?: false
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Publication
11983710 | -
First Author: Bishop AC
Year: 2002
Journal: J Biol Chem
Title: Identification of the tRNA-dihydrouridine synthase family.
Volume: 277
Issue: 28
Pages: 25090-5
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Protein
Q8C2P3
Organism: Mus musculus/domesticus
Length: 475  
Fragment?: false
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Protein
B1ATU5
Organism: Mus musculus/domesticus
Length: 482  
Fragment?: false
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Protein
B1ATU6
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
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Protein
B1ATU7
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: true
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Protein
Q91XI1
Organism: Mus musculus/domesticus
Length: 637  
Fragment?: false
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Protein
A0A0R4IZY9
Organism: Mus musculus/domesticus
Length: 637  
Fragment?: false
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