The C-terminal domain of the largest subunit of RNA polymerase II in higher eukaryotes is present in the protozoan parasite Trypanosoma brucei in a strongly modified form. To determine whether this is a general feature of the Kinetoplastida and to determine the role of this domain in RNA polymerase II transcription, we have analysed the C-terminal domain of the distantly related species Crithidia fasciculata. No positional identity of amino acid residues between the C-termini of C. fasciculata and T. brucei can be found. Moreover, both domains lack the heptapeptide repeat structure present in higher eukaryotes. The two domains are, however, very similar in amino acid composition, being rich in acidic residues as well as serine and tryosine. The latter observation is compatible with the concept that in vivo phosphorylation of the C-terminus activates RNA polymerase II.