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    GLN4 glutamine--tRNA ligase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854339, updated on 9-Dec-2024

    Summary

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    Official Symbol
    GLN4
    Official Full Name
    glutamine--tRNA ligase
    Primary source
    SGD:S000005694
    Locus tag
    YOR168W
    See related
    AllianceGenome:SGD:S000005694; FungiDB:YOR168W; VEuPathDB:YOR168W
    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 glutamine-tRNA ligase activity and sequence-specific mRNA binding activity. Involved in glutaminyl-tRNA aminoacylation. Located in cytosol and mitochondrion. Orthologous to human QARS1 (glutaminyl-tRNA synthetase 1). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See GLN4 in Genome Data Viewer
    Location:
    chromosome: XV
    Exon count:
    1
    Sequence:
    Chromosome: XV; NC_001147.6 (649303..651732)

    Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene mRNA-processing endoribonuclease Neighboring gene ribosomal 40S subunit protein S28A Neighboring gene sphinganine kinase LCB4 Neighboring gene Yrm1p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001147.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Cloning of GLN4: an essential gene that encodes glutaminyl-tRNA synthetase in Saccharomyces cerevisiae. Ludmerer SW, et al. J Bacteriol, 1985 Aug. PMID 2991203, Free PMC Article
    2. Gene for yeast glutamine tRNA synthetase encodes a large amino-terminal extension and provides a strong confirmation of the signature sequence for a group of the aminoacyl-tRNA synthetases. Ludmerer SW, et al. J Biol Chem, 1987 Aug 5. PMID 3301841
    3. Construction and analysis of deletions in the amino-terminal extension of glutamine tRNA synthetase of Saccharomyces cerevisiae. Ludmerer SW, et al. J Biol Chem, 1987 Aug 5. PMID 3301842
    4. Purification of glutamine tRNA synthetase from Saccharomyces cerevisiae. A monomeric aminoacyl-tRNA synthetase with a large and dispensable NH2-terminal domain. Ludmerer SW, et al. J Biol Chem, 1993 Mar 15. PMID 8449914
    5. Rescuing an essential enzyme-RNA complex with a non-essential appended domain. Whelihan EF, et al. EMBO J, 1997 May 15. PMID 9184240, Free PMC Article

    See all (45) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. the eukaryote-specific protein domains of GluRS and GlnRS substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA
      Title: Coevolution of specificity determinants in eukaryotic glutamyl- and glutaminyl-tRNA synthetases.
    2. The structure of the C-terminal domain is highly similar to Escherichia coli GlnRS but 214 residues, including the N-terminal domain, are crystallographically disordered.
      Title: The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA.
    3. A functional and structural analysis of the N-terminal appended domain of Saccharomyces cerevisiae GlnRS, Gln4.
      Title: Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase.
    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 glutamine-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables glutamine-tRNA ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables glutamine-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables mRNA binding HDA PubMed 
    enables sequence-specific mRNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in glutaminyl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in glutaminyl-tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in glutaminyl-tRNA aminoacylation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrion IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    glutamine--tRNA ligase
    NP_014811.3
    • Glutamine tRNA synthetase; monomeric class I tRNA synthetase that catalyzes the specific glutaminylation of tRNA(Gln); N-terminal domain proposed to be involved in enzyme-tRNA interactions

    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_001147.6 Reference assembly

      Range
      649303..651732
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183587.3 → NP_014811.3  TPA: glutamine--tRNA ligase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014811.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W2M6, P13188, Q12005
      UniProtKB/TrEMBL
      A6ZP13, B3LJK1, B5VS54, C7GN56, C8ZGS9, N1P3A6
      Conserved Domains (3) summary
      TIGR00440
      Location:252 → 807
      glnS; glutaminyl-tRNA synthetase
      pfam04557
      Location:166 → 244
      tRNA_synt_1c_R2; Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2
      pfam04558
      Location:5 → 163
      tRNA_synt_1c_R1; Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P13188.2

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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