Genome location: Pf3D7_14_v3:1,370,611..1,375,278(+)
Genome classification: Core
Product Description: Hsp70/Hsp90 organizing protein
SignalP Peptide: N/A
# Transmembrane Domains: 0
EC Numbers: None
Curated GO (PlasmoDB):
Type | GO Term | Name |
---|---|---|
Component | GO:0005829 | cytosol |
Function | GO:0060590 | ATPase regulator activity |
Function | GO:0030544 | Hsp70 protein binding |
Function | GO:0051879 | Hsp90 protein binding |
Function | GO:0005515 | protein binding |
Expression by stage (LR - Le Roch et al., and MCA - Malaria Cell Atlas):
Stage | LR class | MCA mean | MCA prop. zeros |
---|---|---|---|
Sporozoite | not expressed | N/A | N/A |
Ring | expressed | 1.07 | 0.53 |
Trophozoite | expressed | 1.52 | 0.34 |
Schizont | expressed | 0.22 | 0.87 |
Gametocyte | expressed | 0.57 | 0.70 |
More info:
Old (Pf3D7v3) Gene ID: PF3D7_1434300
Resistome Missense Mutations: None
Resistome Compounds with Missense Mutations: None
Resistome # Samples with Disruptive Mutations: 0 (0 missense, 0 "interesting" missense)
Zhang Phenotype: Non - Mutable in CDS
MIS: 0.233 | MFS: -2.873 | #Insertions: 0
PlasmoGEM Phenotype: Dispensable (Pb ortholog: PBANKA_1010500)
RMgmDB ABS Phenotype: Different from wild type (Pb ortholog: PBANKA_1010500)
Modification: Disrupted | RMgm-2762
More info: PhenoPlasm Link
AlphaFill Uniprot ID: Q8ILC1
"Best" AlphaFill ligand hit: GDP (guanosine-5'-diphosphate, Local RMSD=0.21) with 2XKB (Global RMSD=16.27)
No associated EC numbersNo evidence of orthology to BindingDB entries
Ortholog Group (OrthoMCL): OG6_102012
Most Similar Human Ortholog: F5GXD8
TM-align score: 0.88 | RMSD: 1.94
Seq Identity: 0.38 | Length: 133 / 564
All Human Orthologs (OrthoMCL):
Gene ID | Description |
---|---|
ENSG00000168439 | stress induced phosphoprotein 1 |
MalariaGEN Pf7 (worldwide samples) # unique SNV/indels:
Homozygous genotype calls only
variant type | common | rare | doubleton | singleton |
---|---|---|---|---|
synonymous | 3 | 30 | 11 | 31 |
disruptive | 2 | 18 | 15 | 38 |
missense | 2 | 15 | 12 | 37 |
Any inclusion in genotype call
variant type | common | rare | doubleton | singleton |
---|---|---|---|---|
synonymous | 10 | 54 | 25 | 40 |
disruptive | 3 | 54 | 47 | 84 |
missense | 3 | 42 | 40 | 65 |
PlasmoDB Total SNPs: 169
Non-coding: 153 | Synonymous: 10 | Nonsynonymous: 4 | Stop Codon: 2
Protein Length: 564 | Molecular Weight (kDa): 66.057
UniProt ID(s): A0A144A2J9, P25407, Q8ILC1
PDB ID(s): None
Isoelectric Point: 7
Protein Domain Annotations:
Source | Family ID | Description |
---|---|---|
InterPro | IPR001440 | Tetratricopeptide repeat 1 |
InterPro | IPR006636 | Heat shock chaperonin-binding |
InterPro | IPR011990 | Tetratricopeptide-like helical domain superfamily |
InterPro | IPR019734 | Tetratricopeptide repeat |
InterPro | IPR041243 | STI1 domain |
PFam | PF00515 | Tetratricopeptide repeat 1 |
PFam | PF13181 | Tetratricopeptide repeat |
PFam | PF13414 | STI1 domain |
PFam | PF17830 | |
Superfamily | SSF48452 | Tetratricopeptide-like helical domain superfamily |
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 |
22005844 | Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein(PfHop). | Gitau GW, Mandal P, ..., Shonhai A | 10.1007/s12192-011-0299-x |
26267894 | Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in aNucleotide-Dependent Fashion and Exhibits Ligand Selectivity. | Zininga T, Makumire S, ..., Shonhai A | 10.1371/journal.pone.0135326 |
31525467 | Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparumand its modulation of Hsp70 and Hsp90 ATPase activities. | Silva NSM, Bertolino-Reis DE, ..., Borges JC | 10.1016/j.bbapap.2019.140282 |
32343703 | Biophysical analysis of Plasmodium falciparum Hsp70-Hsp90 organising protein(PfHop) reveals a monomer that is characterised by folded segments connected byflexible linkers. | Makumire S, Zininga T, ..., Shonhai A | 10.1371/journal.pone.0226657 |