About Gene List

PF3D7_1417500 (CBF5)

Genome location: Pf3D7_14_v3:726,517..729,371(-)

Genome classification: Core

Function and Localization

Product Description: H/ACA ribonucleoprotein complex subunit 4, putative

SignalP Peptide: N/A

# Transmembrane Domains: 0

EC Numbers: 5.4.99.- (Transferring other groups.)

Curated GO (PlasmoDB):

Type GO Term Name
Component GO:0031429 box H/ACA snoRNP complex
Component GO:0005634 nucleus
Function GO:0009982 pseudouridine synthase activity
Process GO:0000495 box H/ACA RNA 3'-end processing
Process GO:1990481 mRNA pseudouridine synthesis
Process GO:0031118 rRNA pseudouridine synthesis
Process GO:0031120 snRNA pseudouridine synthesis

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 0.63 0.70
Trophozoite expressed 0.44 0.74
Schizont expressed 0.09 0.94
Gametocyte expressed 0.43 0.75

More info:

Resistome Mutations

Old (Pf3D7v3) Gene ID: PF3D7_1417500

Resistome Missense Mutations: None

Resistome Compounds with Missense Mutations: None

Resistome # Samples with Disruptive Mutations: 0 (0 missense, 0 "interesting" missense)

Essentiality (ABS)

Zhang Phenotype: Non - Mutable in CDS

MIS: 0.278 | MFS: -2.691 | #Insertions: 0

PlasmoGEM Phenotype: Essential (Pb ortholog: PBANKA_1025200)

  • Relative Growth Rate: 0.18 ± 0.24
  • Confidence: 4.25

RMgmDB ABS Phenotype: N/A

More info: PhenoPlasm Link

Binding Evidence

AlphaFill Uniprot ID: Q8ILS0

"Best" AlphaFill ligand hit: ATP (adenosine-5'-triphosphate, Local RMSD=2.07) with 2HVY (Global RMSD=2.65)

BRENDA EC Inhibitors:

EC # Name EC Inhibitors
5.4.99.- Ex: tRNA pseudouridine38-40 synthase SDSGTPGDPNEMEDTAtRNAPCMBFeCl2CuSO3HgCl2CuSO4AgNO3...

No evidence of orthology to BindingDB entries

Orthology Information

Ortholog Group (OrthoMCL): OG6_100327

Most Similar Human Ortholog: O60832

TM-align score: 0.85 | RMSD: 2.31

Seq Identity: 0.59 | Length: 413 / 466

All Human Orthologs (OrthoMCL):

Gene ID Description
ENSG00000130826 dyskerin pseudouridine synthase 1
ENSG00000165832 TruB pseudouridine synthase family member 1

Genetic Variation

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

Homozygous genotype calls only

variant type common rare doubleton singleton
synonymous 4 20 15 29
disruptive 4 23 17 35
missense 4 23 11 33

Any inclusion in genotype call

variant type common rare doubleton singleton
synonymous 5 61 15 33
disruptive 11 55 36 89
missense 7 44 31 68

PlasmoDB Total SNPs: 118

Non-coding: 108 | Synonymous: 7 | Nonsynonymous: 3 | Stop Codon: 0

Protein Information

Protein Length: 466 | Molecular Weight (kDa): 52.942

UniProt ID(s): Q8ILS0

PDB ID(s): None

Isoelectric Point: 9.25

Protein Domain Annotations:

Source Family ID Description
InterPro IPR002478 PUA domain
InterPro IPR002501 Pseudouridine synthase II, N-terminal
InterPro IPR004802 tRNA pseudouridine synthase B family
InterPro IPR012960 Dyskerin-like
InterPro IPR015947 PUA-like superfamily
InterPro IPR020103 Pseudouridine synthase, catalytic domain superfamily
InterPro IPR032819 tRNA pseudouridylate synthase B, C-terminal
PFam PF01472 PUA domain
PFam PF01509 Pseudouridine synthase II, N-terminal
PFam PF08068 Dyskerin-like
PFam PF16198 tRNA pseudouridylate synthase B, C-terminal
Superfamily SSF55120 Pseudouridine synthase, catalytic domain superfamily
Superfamily SSF88697 PUA-like superfamily

Associated Publications

PMID Title Authors DOI/Link
12368864 Genome sequence of the human malaria parasite Plasmodium falciparum. Gardner MJ, Hall N, ..., Barrell B 10.1038/nature01097
16267556 A protein interaction network of the malaria parasite Plasmodium falciparum. LaCount DJ, Vignali M, ..., Hughes RE 10.1038/nature04104
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
31311819 Base-pairing interactions between substrate RNA and H/ACA guide RNA modulate thekinetics of pseudouridylation, but not the affinity of substrate binding by H/ACAsmall nucleolar ribonucleoproteins Kelly EK, Czekay DP, Kothe U 10.1261/rna.071043.119
33823543 Eukaryote specific RNA and protein features facilitate assembly and catalysis ofH/ACA snoRNPs Trucks S, Hanspach G, Hengesbach M 10.1093/nar/gkab177
37818102 Human SHQ1 variants R335C and A426V lead to severe ribosome biogenesis defectswhen expressed in yeast Alidou-D'Anjou I, Patel A, Sleiman S, Dragon F 10.3389/fgene.2023.1240416