The domain within your query sequence starts at position 99 and ends at position 259; the E-value for the Dynamin_N domain shown below is 5.4e-25.



PFAM accession number:PF00350
Interpro abstract (IPR022812):

Membrane transport between compartments in eukaryotic cells requires proteins that allow the budding and scission of nascent cargo vesicles from one compartment and their targeting and fusion with another. Dynamins are large GTPases that belong to a protein superfamily [ (PUBMED:15040446) ] that, in eukaryotic cells, includes classical dynamins, dynamin-like proteins, OPA1, Mx proteins, mitofusins and guanylate-binding proteins/atlastins [ (PUBMED:2142876) (PUBMED:2112425) (PUBMED:1532158) (PUBMED:2607176) ], and are involved in the scission of a wide range of vesicles and organelles. They play a role in many processes including budding of transport vesicles, division of organelles, cytokinesis and pathogen resistance.

The minimal distinguishing architectural features that are common to all dynamins and are distinct from other GTPases are the structure of the large GTPase domain (300 amino acids) and the presence of two additional domains; the middle domain and the GTPase effector domain (GED), which are involved in oligomerization and regulation of the GTPase activity.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Dynamin_N