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    MSD1 aspartate--tRNA ligase MSD1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856000, updated on 2-Nov-2024

    Summary

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    Official Symbol
    MSD1
    Official Full Name
    aspartate--tRNA ligase MSD1
    Primary source
    SGD:S000006025
    Locus tag
    YPL104W
    See related
    AllianceGenome:SGD:S000006025; FungiDB:YPL104W; VEuPathDB:YPL104W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    LPG5
    Summary
    Enables aspartate-tRNA ligase activity. Involved in mitochondrial aspartyl-tRNA aminoacylation. Located in mitochondrion. Used to study leukodystrophy. Orthologous to human DARS2 (aspartyl-tRNA synthetase 2, mitochondrial). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See MSD1 in Genome Data Viewer
    Location:
    chromosome: XVI
    Exon count:
    1
    Sequence:
    Chromosome: XVI; NC_001148.4 (355700..357676)

    Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene adenyl-nucleotide exchange factor SSE1 Neighboring gene Syh1p Neighboring gene N-acetylphosphatidylethanolamine-hydrolyzing phospholipase D Neighboring gene Elongator subunit ELP4

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001148.4

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. A missense mutation in the nuclear gene coding for the mitochondrial aspartyl-tRNA synthetase suppresses a mitochondrial tRNA(Asp) mutation. Chiang CS, et al. Nucleic Acids Res, 2000 Apr 1. PMID 10710420, Free PMC Article
    2. An intricate RNA structure with two tRNA-derived motifs directs complex formation between yeast aspartyl-tRNA synthetase and its mRNA. Ryckelynck M, et al. J Mol Biol, 2005 Dec 2. PMID 16257416
    3. tRNA-balanced expression of a eukaryal aminoacyl-tRNA synthetase by an mRNA-mediated pathway. Frugier M, et al. EMBO Rep, 2005 Sep. PMID 16113655, Free PMC Article
    4. Structure and evolution of a group of related aminoacyl-tRNA synthetases. Gatti DL, et al. J Mol Biol, 1991 Apr 5. PMID 2016746
    5. Homology of aspartyl- and lysyl-tRNA synthetases. Gampel A, et al. Proc Natl Acad Sci U S A, 1989 Aug. PMID 2668951, Free PMC Article

    See all (40) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Expression of AspRS is regulated in yeast by a feedback mechanism that necessitates the binding of AspRS to its messenger RNA.
      Title: tRNA-balanced expression of a eukaryal aminoacyl-tRNA synthetase by an mRNA-mediated pathway.
    2. N-terminal extension of each aspartyl-tRNA synthetase subunit plays a crucial role in anchoring the tRNA-like motifs of the mRNA on the synthetase
      Title: An intricate RNA structure with two tRNA-derived motifs directs complex formation between yeast aspartyl-tRNA synthetase and its mRNA.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    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 ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables aminoacyl-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables aspartate-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables aspartate-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables aspartate-tRNA ligase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables aspartate-tRNA ligase activity ISA
    Inferred from Sequence Alignment
    more info
    		 PubMed 
    enables nucleic acid binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in aspartyl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in mitochondrial aspartyl-tRNA aminoacylation IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in mitochondrial aspartyl-tRNA aminoacylation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tRNA aminoacylation for protein translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrial matrix IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    aspartate--tRNA ligase MSD1
    NP_015221.1
    • Mitochondrial aspartyl-tRNA synthetase; required for acylation of aspartyl-tRNA; yeast and bacterial aspartyl-, asparaginyl-, and lysyl-tRNA synthetases contain regions with high sequence similarity, suggesting a common ancestral gene

    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_001148.4 Reference assembly

      Range
      355700..357676
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183918.1 → NP_015221.1  TPA: aspartate--tRNA ligase MSD1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_015221.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W3R3, P15179
      UniProtKB/TrEMBL
      A6ZWE7, B3LKW9, N1NVG9
      Conserved Domains (1) summary
      TIGR00459
      Location:35 → 658
      aspS_bact; aspartyl-tRNA synthetase, bacterial type
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P15179.1

    Gene LinkOut

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