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Search results 101 to 114 out of 114 for Tyw1

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0.018s
Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 721  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 386  
Fragment?: false
Publication
First Author: Suzuki Y
Year: 2007
Journal: J Mol Biol
Title: Crystal structure of the radical SAM enzyme catalyzing tricyclic modified base formation in tRNA.
Volume: 372
Issue: 5
Pages: 1204-14
Protein Domain
Type: Family
Description: Members of this protein family are the archaeal protein TYW1 [], a radical SAM protein that catalyzes the second step in creating the wye-bases, wyosine and derivatives such as wybutosine, for tRNA base modification [].
Publication
First Author: Goto-Ito S
Year: 2007
Journal: Acta Crystallogr D Biol Crystallogr
Title: Structure of an archaeal TYW1, the enzyme catalyzing the second step of wye-base biosynthesis.
Volume: 63
Issue: Pt 10
Pages: 1059-68
Publication
First Author: Yang Z
Year: 2004
Journal: J Mol Biol
Title: Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase.
Volume: 340
Issue: 4
Pages: 695-706
Publication
First Author: Young AP
Year: 2011
Journal: Biochemistry
Title: Pyruvate is the source of the two carbons that are required for formation of the imidazoline ring of 4-demethylwyosine.
Volume: 50
Issue: 49
Pages: 10573-5
Protein Domain
Type: Family
Description: This entry respresents S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase Tyw1 from eukaryotes and archaea. They are involved in the pathway wybutosine-tRNA(Phe) biosynthesis. It binds one [4Fe-4S]cluster and one [2Fe-2S]cluster. The [4Fe-4S]cluster is coordinated with three cysteines and an exchangeable S-adenosyl-L-methionine [, ]. The two carbon source required for this reaction has been identified as pyruvate. The exact role of the SAM molecule has yet to be determined. There appear to be two distinct sets of proteins with different multi-domain architectures, however they are sufficiently similar in the Radical SAM portion that they remain a single cluster [].Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. It is important for translational reading-frame maintenance [].
Publication
First Author: Noma A
Year: 2006
Journal: EMBO J
Title: Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA.
Volume: 25
Issue: 10
Pages: 2142-54
Publication
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
Publication
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89
Publication
First Author: Church DM
Year: 2009
Journal: PLoS Biol
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume: 7
Issue: 5
Pages: e1000112