A type-1 metacaspase from Acanthamoeba castellanii.
The complete sequence of a type-1 metacaspase from Acanthamoeba castellanii is reported comprising 478 amino acids. The metacaspase was recovered from an expression library using sera specific for membrane components implicated in stimulating encystation. A central domain of 155 amino acid residues contains the Cys/His catalytic dyad and is the most conserved region containing at least 30 amino acid identities in all metacaspases. The Acanthamoeba castellanii metacaspase has the most proline-rich N-terminus so far reported in type-1 metacaspases with over 40 prolines in the first 150 residues. Ala-Pro-Pro is present 11 times. Phylogenies constructed using only the conserved proteolytic domains or the complete sequences show identical branching patterns, differing only in the rates of change.
Trzyna
Wendy C
WC
Department of Biological Sciences, Louisiana Tech University, Ruston, LA 71272, USA. wtrzyna@latech.edu <wtrzyna@latech.edu>
Legras
Xavier D
XD
Cordingley
John S
JS
D048248:Acanthamoeba castellanii / Q000201:enzymology* / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D020169:Caspases / Q000737:chemistry / Q000235:genetics*; D020134:Catalytic Domain; D017124:Conserved Sequence; D016054:DNA, Protozoan / Q000737:chemistry / Q000235:genetics; D008969:Molecular Sequence Data; D010802:Phylogeny; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
D016054:DNA, Protozoan; D020169:Caspases