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Motor proteins of cytoplasmic microtubules.
ANNU.REV.BIOCHEMISTRY 59 909-932 (1990).
2. ROTHMAN, J.H., RAYMOND, C.K., GILBERT, T., O'HARA, P.J. AND
A putative GTP-binding protein homologous to interferon-inducible Mx
proteins performs an essential function in yeast protein sorting.
CELL 61 1063-1074 (1990).
3. JONES, B.A. AND FANGMAN, W.L.
Mitochondrial DNA maintenance in yeast requires a protein containing a
region related to the GTP-binding domain of dynamin.
GENES DEV. 6 380-389 (1992).
4. WEITZ, G., BEKISZ, J., ZOON, K. AND ARNHEITER, H.
Purification and characterisation of a human Mx protein.
J.INTERFERON RES. 9(6) 679-689 (1989).
Dynamin is a microtubule-associated, force-producing protein involved in
the production of microtubule bundles . It is structurally related to
yeast vacuolar sorting protein , yeast MGM1 protein  and interferon-
induced Mx proteins . These proteins all hydrolyse GTP, each containing
motifs common to all GTP-binding proteins towards their N-termini.
DYNAMIN is a 6-element fingerprint that provides a signature for the
dynamins and related proteins. The fingerprint was derived from an initial
alignment of 7 sequences: the motifs were drawn from conserved regions
spanning the N-terminal third of the alignment, motif 2 including the
region encoded by PROSITE pattern DYNAMIN (PS00410), which lies downstream
of the ATP/GTP-binding P-loop. Two iterations on OWL25.2 were required to
reach convergence, at which point a true set comprising 29 sequences was
An update on SPTR37_9f identified a true set of 49 sequences, and 2