Mutant/mutation
The mutant lacks expression of PypPK1

Protein (function)
PY17X_1220300 encodes a 319 amino acid protein with an expected molecular weight of 38 kDa. The CD-Search webware predicted a protein kinase catalytic domain from amino acid positions (aa) 36 to 278 (E-value = 6.63e-22), and a signal peptide sequence or transmembrane region was not predicted. An active protein kinase has several critical features for phosphorylation activity such as a catalytic aspartate and a Mg binding site. The corresponding regions of PY17X_1220300 were not conserved with the known P. yoelii protein kinases, PyCDPK4, PyCDPK3, PyPKAc, PyGSK3, and PyMAPK2, suggesting that PY17X_1220300 does not possess phosphorylation activity. The relevant regions are widely conserved within orthologs in other Plasmodium spp., suggesting that PY17X_1220300 is a pseudokinase with a conserved role across Plasmodium. Taken together, we designated this protein as P. yoelii pseudo Protein Kinase 1 (PypPK1)

Phenotype
Reduced growth/multiplication of asexual blood stages. Evidence is provided for reduced invasion of merozoites.
Normal production of male and female gametocytes. Normal egress of both male and female gametocytes from their host red blood cells after activation. Normal exflagellation rate (i.e. male gamete formation); however, exflagellating males showed (strongly) reduced formation of the characteristic exflagellation centers, i.e. exflagellating males surrounded/attached to uninfected cells.
Strongly reduces formation of oocysts

Additional information
By analyzing a mutant expressing a C-terminal cmyc-tagged version of PypPK1 (RMgm-4709) evidence is presented that PypPK1 is localized at the apical side of daughter merozoites. evidence is presented for presence of protein in nuclei of both male and female gametocytes. and male gametes. Evidence is presented for plasma location of the protein in ookinetes.

Other mutants