About Gene List

PF3D7_0211800 (AsnRS)

Genome location: Pf3D7_02_v3:475,109..477,618(+)

Genome classification: Core

Function and Localization

Product Description: asparagine--tRNA ligase

SignalP Peptide: N/A

# Transmembrane Domains: 0

EC Numbers: 6.1.1.22 (Asparagine--tRNA ligase)

Curated GO (PlasmoDB):

Type GO Term Name
Component GO:0005634 nucleus
Function GO:0004816 asparagine-tRNA ligase activity
Process GO:0006421 asparaginyl-tRNA aminoacylation

Expression by stage (LR - Le Roch et al., and MCA - Malaria Cell Atlas):

Stage LR class MCA mean MCA prop. zeros
Sporozoite expressed N/A N/A
Ring expressed 0.48 0.78
Trophozoite expressed 1.09 0.45
Schizont expressed 0.29 0.81
Gametocyte expressed 0.53 0.70

More info:

Resistome Mutations

Old (Pf3D7v3) Gene ID: PF3D7_0211800

Resistome Missense Mutations: R487S

Resistome Compounds with Missense Mutations: OSM-S-106

Resistome # Samples with Disruptive Mutations: 2 (2 missense, 2 "interesting" missense)

Essentiality (ABS)

Zhang Phenotype: Non - Mutable in CDS

MIS: 0.184 | MFS: -2.765 | #Insertions: 0

PlasmoGEM Phenotype: Essential (Pb ortholog: PBANKA_1109200)

  • Relative Growth Rate: 0.23 ± 0.51
  • Confidence: 2.73

RMgmDB ABS Phenotype: Different from wild type (Pb ortholog: PBANKA_0308600)

Modification: Disrupted | RMgm-1781

More info: PhenoPlasm Link

Binding Evidence

AlphaFill Uniprot ID: O96198

"Best" AlphaFill ligand hit: DSZ (5'-o-(l-alpha-aspartylsulfamoyl)adenosine, Local RMSD=0.55) with 6SJC (Global RMSD=5.69)

BRENDA EC Inhibitors:

EC # Name EC Inhibitors
6.1.1.22 asparagine-tRNA ligase 3D6NH4+NO3-CNS-LCM01LCM02CH3COO-NSC12156NSC35467NSC114691NSC363624variolin B...

No evidence of orthology to BindingDB entries

Orthology Information

Ortholog Group (OrthoMCL): OG6_101288

Most Similar Human Ortholog: Q96I59

TM-align score: 0.90 | RMSD: 1.91

Seq Identity: 0.41 | Length: 449 / 610

All Human Orthologs (OrthoMCL):

Gene ID Description
ENSG00000137513 asparaginyl-tRNA synthetase 2, mitochondrial

Genetic Variation

MalariaGEN Pf7 (worldwide samples) # unique SNV/indels:

Homozygous genotype calls only

variant type common rare doubleton singleton
synonymous 2 38 13 42
disruptive 8 29 15 61
missense 7 25 15 54

Any inclusion in genotype call

variant type common rare doubleton singleton
synonymous 4 78 17 43
disruptive 12 71 40 105
missense 7 59 37 74

PlasmoDB Total SNPs: 73

Non-coding: 54 | Synonymous: 15 | Nonsynonymous: 4 | Stop Codon: 0

Protein Information

Protein Length: 610 | Molecular Weight (kDa): 70.498

UniProt ID(s): O96198

PDB ID(s): None

Isoelectric Point: 6.62

Protein Domain Annotations:

Source Family ID Description
InterPro IPR002312 Aspartyl/Asparaginyl-tRNA synthetase, class IIb
InterPro IPR004364 Aminoacyl-tRNA synthetase, class II (D/K/N)
InterPro IPR004365 OB-fold nucleic acid binding domain, AA-tRNA synthetase-type
InterPro IPR004522 Asparagine-tRNA ligase
InterPro IPR012340 Nucleic acid-binding, OB-fold
PFam PF00152 Aminoacyl-tRNA synthetase, class II (D/K/N)
PFam PF01336 OB-fold nucleic acid binding domain, AA-tRNA synthetase-type
Superfamily SSF50249 Nucleic acid-binding, OB-fold
Superfamily SSF55681

Associated Publications

PMID Title Authors DOI/Link
9804551 Chromosome 2 sequence of the human malaria parasite Plasmodium falciparum. Gardner MJ, Tettelin H, ..., Hoffman SL 10.1126/science.282.5391.1126
12368864 Genome sequence of the human malaria parasite Plasmodium falciparum. Gardner MJ, Hall N, ..., Barrell B 10.1038/nature01097
23181666 Organellar proteomics reveals hundreds of novel nuclear proteins in the malariaparasite Plasmodium falciparum. Oehring SC, Woodcroft BJ, ..., Voss TS 10.1186/gb-2012-13-11-r108
24196969 Aminoacylation of Plasmodium falciparum tRNA(Asn) and insights in the synthesisof asparagine repeats. Filisetti D, Theobald-Dietrich A, ..., Frugier M 10.1074/jbc.M113.522896
30379851 Identification of Plasmodium falciparum nuclear proteins by mass spectrometry andproposed protein annotation. Briquet S, Ourimi A, ..., Vaquero C 10.1371/journal.pone.0205596
37546892 Reaction hijacking inhibition of Plasmodium falciparum asparagine tRNAsynthetase Xie SC, Wang Y, ..., Tilley L 10.21203/rs.3.rs-3198291/v1
37572327 Solution structure of the N-terminal extension domain of a Schistosoma japonicumasparaginyl-tRNA synthetase Peck Y, Pickering D, ..., Daly NL 10.1080/07391102.2023.2241918
26804570 The Bacillus subtilis and Bacillus halodurans Aspartyl-tRNA Synthetases RetainRecognition of tRNA(Asn) Nair N, Raff H, ..., Sheppard K 10.1016/j.jmb.2016.01.014
28180287 The complex evolutionary history of aminoacyl-tRNA synthetases Chaliotis A, Vlastaridis P, ..., Amoutzias GD 10.1093/nar/gkw1182
27223819 Aminoacyl-tRNA Synthetases in the Bacterial World Giege R, Springer M 10.1128/ecosalplus.ESP-0002-2016
33528599 Structural and Genetic Determinants of Convergence in the Drosophila tRNAStructure-Function Map Phillips JB, Ardell DH 10.1007/s00239-021-09995-z
35634293 Aminoacyl-tRNA Synthetases: On Anti-Synthetase Syndrome and Beyond Galindo-Feria AS, Notarnicola A, Lundberg IE, Horuluoglu B 10.3389/fimmu.2022.866087
38297033 Reaction hijacking inhibition of Plasmodium falciparum asparagine tRNAsynthetase Xie SC, Wang Y, ..., Tilley L 10.1038/s41467-024-45224-z
30919766 Spectroscopic Studies of Asparaginyl-tRNA Synthetase from Entamoeba histolytica Biswas P, Sahu DK, Sahu K, Banerjee R 10.2174/0929866526666190327122419