A P-type ATPase From the Aquatic Fungus Blastocladiella Emersonii Similar to Animal Na,K-ATPases

Biochim Biophys Acta. 1998 Apr 2;1383(2):183-7. doi: 10.1016/s0167-4838(97)00221-5.

Abstract

We have cloned a P-type ATPase gene from the aquatic fungus Blastocladiella emersonii (BePAT1) using a probe obtained with degenerate oligonucleotides, corresponding to two amino acid sequences highly conserved among all P-type ATPase isoforms, and the polymerase chain reaction technique. Nucleotide sequence analysis revealed a 3.4 kb open reading frame encoding a putative peptide of 1080 amino acid residues with a calculated molecular mass of 119 kDa, which presents all diagnostic features of P-type transporting ATPases. Comparison to other members of the family and phylogenetic analyses have shown that the BePAT1 protein belongs to the subfamily of Na,K- and H,K-ATPases, indicating that the divergence between the alpha-subunit of the Na,K-ATPase and other members of the P-type ATPase family has occurred before the divergence between the animal and fungal lineages in evolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / genetics*
  • Amino Acid Sequence
  • Animals
  • Blastocladiella / genetics*
  • Evolution, Molecular
  • Molecular Sequence Data
  • Sequence Alignment
  • Sequence Analysis
  • Sequence Homology, Amino Acid
  • Sodium-Potassium-Exchanging ATPase / genetics*

Substances

  • Adenosine Triphosphatases
  • Sodium-Potassium-Exchanging ATPase

Associated data

  • GENBANK/AJ001045