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. 2009 Apr 24;284(17):11590–11600. doi: 10.1074/jbc.M807279200

FIGURE 1.

FIGURE 1.

Sequence analysis of TbPRMT7. A, ClustalW derived cladogram of TbPRMT7 compared with the seven active human PRMTs as well as the uncharacterized PRMT9(4q31) protein. The human PRMTs are grouped as Type I (ADMA catalyzing), Type II (SDMA catalyzing), and the less definitively characterized Type II or III (solely MMA catalyzing) PRMT7. TbPRMT7 is indicated by the arrow. B, domain structure of human PRMT7 compared with that of TbPRMT7. Four closely spaced vertical lines indicate AdoMet binding (or AdoMet binding-like, see text) domains; single vertical line indicates “THW” loops. The degree of homology between TbPRMT7 and human PRMT7 in the most conserved region (spanning 248 amino acids; indicated by the horizontal line) is shown above the diagram. The percent identity and similarity in this region is indicated. C, ClustalW alignment of TbPRMT7 with the N-terminal methyltransferase motifs of PRMT7 homologues from humans (HsPRMT7N (GenBank™ accession number NP_061896)) and Drosophila (DmDart7N (GenBank™ accession number NP_611753)). White letters on black background, identical; white letters on gray background, conserved. Asterisks indicate the conserved glutamate residues of the double E loop.