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    DUS3 tRNA dihydrouridine synthase DUS3 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851117, updated on 9-Dec-2024

    Summary

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    Official Symbol
    DUS3
    Official Full Name
    tRNA dihydrouridine synthase DUS3
    Primary source
    SGD:S000004393
    Locus tag
    YLR401C
    See related
    AllianceGenome:SGD:S000004393; FungiDB:YLR401C; VEuPathDB:YLR401C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables tRNA dihydrouridine synthase activity. Involved in tRNA modification. Located in nuclear periphery. Orthologous to human DUS3L (dihydrouridine synthase 3 like). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See DUS3 in Genome Data Viewer
    Location:
    chromosome: XII
    Exon count:
    1
    Sequence:
    Chromosome: XII; NC_001144.5 (922442..924448, complement)

    Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene SKI complex RNA helicase subunit SKI2 Neighboring gene chromatin-binding protein BDF1 Neighboring gene zinc-coordinating transcription factor SFP1 Neighboring gene seipin

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001144.5

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The specificities of four yeast dihydrouridine synthases for cytoplasmic tRNAs. Xing F, et al. J Biol Chem, 2004 Apr 23. PMID 14970222
    2. Global regulatory functions of Oaf1p and Pip2p (Oaf2p), transcription factors that regulate genes encoding peroxisomal proteins in Saccharomyces cerevisiae. Karpichev IV, et al. Mol Cell Biol, 1998 Nov. PMID 9774671, Free PMC Article
    3. The yeast rapid tRNA decay pathway competes with elongation factor 1A for substrate tRNAs and acts on tRNAs lacking one or more of several modifications. Dewe JM, et al. RNA, 2012 Oct. PMID 22895820, Free PMC Article
    4. Rapid tRNA decay can result from lack of nonessential modifications. Alexandrov A, et al. Mol Cell, 2006 Jan 6. PMID 16387656
    5. Degradation of several hypomodified mature tRNA species in Saccharomyces cerevisiae is mediated by Met22 and the 5'-3' exonucleases Rat1 and Xrn1. Chernyakov I, et al. Genes Dev, 2008 May 15. PMID 18443146, Free PMC Article

    See all (43) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables flavin adenine dinucleotide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables mRNA binding HDA PubMed 
    enables mRNA dihydrouridine synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables tRNA dihydrouridine synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables tRNA dihydrouridine synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables tRNA dihydrouridine synthase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables tRNA-dihydrouridine47 synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in mRNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA dihydrouridine synthesis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA modification IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tRNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nuclear periphery IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus HDA PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    tRNA dihydrouridine synthase DUS3
    NP_013505.4
    • Dihydrouridine synthase; member of a widespread family of conserved proteins including Smm1p, Dus1p, and Dus4p; modifies pre-tRNAs at U47 of the variable arm; contains a consensus oleate response element (ORE) in its promoter region; forms nuclear foci upon DNA replication stress

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001144.5 Reference assembly

      Range
      922442..924448 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182289.3 → NP_013505.4  TPA: tRNA dihydrouridine synthase DUS3 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013505.4

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      A7A1S5, D6VZ35, P39519, Q06053
      UniProtKB/TrEMBL
      B5VNT6, C7GXK4, G2WJL5, N1P064
      Conserved Domains (2) summary
      COG0042
      Location:284 → 597
      DusA; tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]
      pfam18044
      Location:96 → 120
      zf-CCCH_4; CCCH-type zinc finger
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q06053.2

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