U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    PF3D7_0925300 proline--tRNA ligase, putative [ Plasmodium falciparum 3D7 ]

    Gene ID: 813528, updated on 12-Sep-2024

    Summary

    Go to the top of the page Help
    Gene symbol
    PF3D7_0925300
    Gene description
    proline--tRNA ligase, putative
    Locus tag
    PF3D7_0925300
    See related
    PlasmoDB:PF3D7_0925300; VEuPathDB:PF3D7_0925300
    Gene type
    protein coding
    RNA name
    proline--tRNA ligase, putative
    RefSeq status
    PROVISIONAL
    Organism
    Plasmodium falciparum 3D7 (isolate: 3D7)
    Lineage
    Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; Plasmodiidae; Plasmodium; Plasmodium (Laverania)
    Orthologs
    all
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    See PF3D7_0925300 in Genome Data Viewer
    Location:
    chromosome: 9
    Exon count:
    1
    Sequence:
    Chromosome: 9; NC_004330.2 (1019164..1020903, complement)

    Chromosome 9 - NC_004330.2Genomic Context describing neighboring genes Neighboring gene conserved Plasmodium protein, unknown function Neighboring gene ribosomal RNA-processing protein 8, putative Neighboring gene protein phosphatase-beta Neighboring gene thioredoxin-like protein 2

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_004330.2

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. The cytoplasmic prolyl-tRNA synthetase of the malaria parasite is a dual-stage target of febrifugine and its analogs. Herman JD, et al. Sci Transl Med, 2015 May 20. PMID 25995223, Free PMC Article
    2. Structural and functional analysis of the anti-malarial drug target prolyl-tRNA synthetase. Jain V, et al. J Struct Funct Genomics, 2014 Dec. PMID 25047712
    3. Integrative proteomics and bioinformatic prediction enable a high-confidence apicoplast proteome in malaria parasites. Boucher MJ, et al. PLoS Biol, 2018 Sep. PMID 30212465, Free PMC Article
    4. A Prioritized and Validated Resource of Mitochondrial Proteins in Plasmodium Identifies Unique Biology. van Esveld SL, et al. mSphere, 2021 Oct 27. PMID 34494883, Free PMC Article
    5. Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13. Hall N, et al. Nature, 2002 Oct 3. PMID 12368867

    GeneRIFs: Gene References Into Functions

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by GeneDB

    Component Evidence Code Pubs
    located_in apicoplast HDA PubMed 
    located_in mitochondrion RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 

    General protein information

    Go to the top of the page Help
    Preferred Names
    proline--tRNA ligase, putative
    XP_001352123.1

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_004330.2 Reference assembly

      Range
      1019164..1020903 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_001352087.1 → XP_001352123.1  proline--tRNA ligase, putative [Plasmodium falciparum 3D7]

      See identical proteins and their annotated locations for XP_001352123.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A024VWN0, A0A024X9W8, A0A0L7K8J8, A0A2I0BS97, Q8I2Q5, W4IZG6, W7FR70, W7JYQ7
      Conserved Domains (2) summary
      cl00266
      Location:477 → 572
      HGTP_anticodon; HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for ...
      cl00268
      Location:79 → 346
      class_II_aaRS-like_core; Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches ...
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

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

    Molecular Biology Databases
    Research Materials