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. 1999 Jan;10(1):225–243. doi: 10.1091/mbc.10.1.225

Figure 1.

Figure 1

Sequence analysis of D. discoideum dynamin A. (A) Predicted amino acid sequence of dynamin A. Dynamin A has a calculated molecular mass of 96.1 kDa and an isoelectric point of 7.0. The tripartite GTP-binding motif is underlined. (B) Sequence alignment of the GTP-binding domains of D. discoideum dynamin A (top), human dynamin-1 (middle), and yeast Dnm1p (bottom). An insert in the Dnm1p sequence corresponding to residues 73–114 was omitted from the alignment. The position of the insert is marked by an X in the alignment. Gaps are presented as —. (C) Sequence alignment of the putative GTPase effector domains of dynamin A, human dynamin-1, and the shibire gene product. (D) Diagram of dynamin A structural domains. The GTPase domain is shown in solid black, and the tripartite GTP-binding motif is indicated as white bars. LZ, leucine zipper; GED, GTPase effector domain; QNS, glutamine-asparagine-serine-rich domain. The basic, proline-rich part of the QNS-rich region, corresponding to residues 573 to 624, is shown in dark gray.