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GLN4 glutamine--tRNA ligase [ Saccharomyces cerevisiae S288C ]

Gene ID: 854339, updated on 13-Apr-2024

Summary

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Gene symbol
GLN4
Gene description
glutamine--tRNA ligase
Primary source
SGD:S000005694
Locus tag
YOR168W
See related
AllianceGenome:SGD:S000005694
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. Involved in glutaminyl-tRNA aminoacylation. Located in cytosol and mitochondrion. Orthologous to human QARS1 (glutaminyl-tRNA synthetase 1). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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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. The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA. Grant TD, et al. J Mol Biol, 2013 Jul 24. PMID 23583912, Free PMC Article
  2. 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
  3. 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
  4. 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
  5. 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

See all (40) 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
    A0A8H4BUZ5, 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

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