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prs1 proline--tRNA (Pro) ligase Prs1 [ Schizosaccharomyces pombe (fission yeast) ]

Gene ID: 2540431, updated on 18-Sep-2024

Summary

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Official Symbol
prs1
Official Full Name
proline--tRNA (Pro) ligase Prs1
Primary source
PomBase:SPBC19C7.06
Locus tag
SPOM_SPBC19C7.06
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Schizosaccharomyces pombe (strain: 972h-)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces
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Genomic context

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See prs1 in Genome Data Viewer
Location:
chromosome: II
Exon count:
1
Sequence:
Chromosome: II; NC_003423.3 (2831790..2834130)

Chromosome II - NC_003423.3Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene protein Rcr1 Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene tRNA-splicing endonuclease catalytic subunit Sen34 Neighboring gene ncRNA Neighboring gene tRNA methyltransferase Ppm2

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_003423.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. tRNA production links nutrient conditions to the onset of sexual differentiation through the TORC1 pathway. Otsubo Y, et al. EMBO Rep, 2018 Mar. PMID 29330317, Free PMC Article
  2. Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions. Nie M, et al. J Biol Chem, 2012 Aug 24. PMID 22730331, Free PMC Article
  3. Proximity-dependent biotinylation mediated by TurboID to identify protein-protein interaction networks in yeast. Larochelle M, et al. J Cell Sci, 2019 May 31. PMID 31064814
  4. Predicting the fission yeast protein interaction network. Pancaldi V, et al. G3 (Bethesda), 2012 Apr. PMID 22540037, Free PMC Article
  5. A non-transcriptional role for the glucocorticoid receptor in mediating the cell stress response. Ptushkina M, et al. Sci Rep, 2017 Sep 21. PMID 28935859, Free PMC Article

See all (13) 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 PomBase

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables Cys-tRNA(Pro) hydrolase activity ISM
Inferred from Sequence Model
more info
  
enables proline-tRNA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
Process Evidence Code Pubs
involved_in cytoplasmic translation NAS
Non-traceable Author Statement
more info
  
involved_in prolyl-tRNA aminoacylation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in prolyl-tRNA aminoacylation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
part_of aminoacyl-tRNA synthetase multienzyme complex IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in cytosol HDA PubMed 

General protein information

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Preferred Names
proline--tRNA (Pro) ligase Prs1

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_003423.3 Reference assembly

    Range
    2831790..2834130
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001022082.3 → NP_596162.1  proline--tRNA (Pro) ligase Prs1 [Schizosaccharomyces pombe]

    See identical proteins and their annotated locations for NP_596162.1

    Status: PROVISIONAL

    UniProtKB/Swiss-Prot
    O60155
    Conserved Domains (4) summary
    PRK08661
    Location:202 → 716
    PRK08661; prolyl-tRNA synthetase; Provisional
    cd00778
    Location:214 → 483
    ProRS_core_arch_euk; Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of ...
    cd00862
    Location:489 → 716
    ProRS_anticodon_zinc; ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in ...
    pfam04073
    Location:33 → 156
    tRNA_edit; Aminoacyl-tRNA editing domain
Nucleotide Protein
Heading Accession and Version

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Molecular Biology Databases
Research Materials