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    arginine--tRNA ligase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851942, updated on 9-Dec-2024

    Summary

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    Official Full Name
    arginine--tRNA ligase
    Primary source
    SGD:S000002749
    Locus tag
    YDR341C
    See related
    AllianceGenome:SGD:S000002749; FungiDB:YDR341C; VEuPathDB:YDR341C
    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
    RRS1
    Summary
    Enables arginine-tRNA ligase activity and sequence-specific mRNA binding activity. Involved in arginyl-tRNA aminoacylation. Located in mitochondrion. Human ortholog(s) of this gene implicated in pontocerebellar hypoplasia type 6. Orthologous to human RARS2 (arginyl-tRNA synthetase 2, mitochondrial). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    Location:
    chromosome: IV
    Exon count:
    1
    Sequence:
    Chromosome: IV; NC_001136.10 (1151803..1153626, complement)

    Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene rRNA-processing protein FCF1 Neighboring gene tRNA-Ser Neighboring gene hexose transporter HXT7 Neighboring gene hexose transporter HXT6

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001136.10

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Limited set of amino acid residues in a class Ia aminoacyl-tRNA synthetase is crucial for tRNA binding. Geslain R, et al. Biochemistry, 2003 Dec 30. PMID 14690419
    2. Mirror image alternative interaction patterns of the same tRNA with either class I arginyl-tRNA synthetase or class II aspartyl-tRNA synthetase. Sissler M, et al. Nucleic Acids Res, 1997 Dec 15. PMID 9396794, Free PMC Article
    3. In vivo selection of lethal mutations reveals two functional domains in arginyl-tRNA synthetase. Geslain R, et al. RNA, 2000 Mar. PMID 10744027, Free PMC Article
    4. The RNA sequence context defines the mechanistic routes by which yeast arginyl-tRNA synthetase charges tRNA. Sissler M, et al. RNA, 1998 Jun. PMID 9622124, Free PMC Article
    5. Crystallization and preliminary X-ray crystallographic analysis of yeast arginyl-tRNA synthetase-yeast tRNAArg complexes. Delagoutte B, et al. Acta Crystallogr D Biol Crystallogr, 2000 Apr. PMID 10739930

    See all (46) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 arginine-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables arginine-tRNA ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables arginine-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables sequence-specific mRNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in arginyl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in arginyl-tRNA aminoacylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in arginyl-tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in mitochondrial translation IBA
    Inferred from Biological aspect of Ancestor
    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 cytosol 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
    		  

    General protein information

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    Preferred Names
    arginine--tRNA ligase
    NP_010628.3
    • Arginyl-tRNA synthetase; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; YDR341C has a paralog, MSR1, that arose from the whole genome duplication

    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_001136.10 Reference assembly

      Range
      1151803..1153626 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180649.3 → NP_010628.3  TPA: arginine--tRNA ligase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010628.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VSX2, Q05506
      UniProtKB/TrEMBL
      A6ZYU2, C7GVV2, N1P779
      Conserved Domains (1) summary
      TIGR00456
      Location:31 → 607
      argS; arginyl-tRNA synthetase
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q05506.1

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