Taxonomic distribution of proteins containing AAI domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing AAI domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Phospholipid transfer proteins.

Wirtz KW
Annu Rev Biochem. 1991; 60: 73-99

Cloning and characterization of a cDNA encoding the wheat (Triticum durum Desf.) CM16 protein.

Gautier MF, Alary R, Joudrier P
Plant Mol Biol. 1990; 14: 313-22

A Triticum durum cDNA library prepared from developing endosperm (22 days after flowering (DAF] was screened using synthetic oligonucleotide probes covering part of the CM3 and CM16 N-terminal protein sequences. A full-length cDNA clone (pTd78) encoding the CM16 protein (chloroform/methanol-soluble protein) was isolated and characterized. To our knowledge this is the first characterization of a clone coding for a wheat CM protein. The CM16 protein is synthesized as a preprotein with a signal peptide of 24 residues, the molecular weight of the mature protein being 13,438 Da. As other members of the cereal trypsin/alpha-amylase inhibitor family, the CM16 protein contains 10 cysteine residues, their position being well conserved. In developing endosperm the highest level of CM16 mRNA was detected at mid-maturation.

Hydrophobic-cluster analysis of plant protein sequences. A domain homology between storage and lipid-transfer proteins.

Henrissat B, Popineau Y, Kader JC
Biochem J. 1988; 255: 901-5

Hydrophobic-cluster analysis was used to characterize a conserved domain located near the C-terminal amino acid sequence of wheat (Triticum aestivum) storage proteins. This domain was transformed into a linear template for a global search for similarities in over 5200 protein sequences. In addition to proteins that had already been found to exhibit homology to wheat storage proteins, a previously unreported homology was found with non-specific lipid-transfer proteins from castor bean (Ricinus communis) and from spinach (Spinacia oleracea) leaf. Hydrophobic-cluster analysis of various members of the present protein group clearly shows a typical domain structure where (i) variable and conserved domains are located along the sequence at precise positions, (ii) the conserved domains probably reflect a common ancestor, and (iii) the unique properties of a given protein (chain cut into subunits, repetitive domains, trypsin-inhibitor active site) are associated with the variable domains.