The domain within your query sequence starts at position 67 and ends at position 435; the E-value for the JMY domain shown below is 1.3e-157.

WAGVLSPAGFRGAHRQLAALWPALEPCFPPLPPELDAASGAGWGLGRGLWALLWPLLWPA
PADPGDSALQELCRQLEHYLGLAAEGCGGATVRDVLFPAPGDSADCEGLSEFRERTLRAR
LGQTATRLHQVLQDHGKANTMVALMKVYQEEDELYQELVTMATTFFQYLLQPFRDMREVA
TSCKLGILKSLDEDELGPRRVAALQKEASEWTRQAEEAVGSIQDITVNYFKETVTALTGM
QKQMEQDQKRFGQAAWATAMPRLENLKLMLARETLQLMRAKELCLKHRQAEIQRKVEDLP
RQGKQLDVVDELEIQCYEIQLELYDVKLEMLRNEETILVTRLDSVKRLITEKQAEVIYYD
PCESPEELQ

JMY

JMY
PFAM accession number:PF15871
Interpro abstract (IPR031738):

JMY (junction-mediating and -regulatory protein) [(PUBMED:19287377)] and WHAMM (WASP homologue-associated protein with actin, membranes and microtubules) [(PUBMED:18614018)] are two nucleation-promoting factors (NPFs) with similar domain architecture. JMY was originally identified as a transcriptional co-factor in the p53-response to DNA damage. Aside from this nuclear function, JMY is involved in cytoskeleton remodelling and trans-Golgi transport [(PUBMED:25015719)]. WHAMM binds microtubules and is involved in ER to cis-Golgi transport [(PUBMED:18614018)]. JMY and WHAMM show similar localisation and could be involved in similar processes [(PUBMED:26096974)].

This middle domain is the coiled-coil region that putatively binds microtubules to the scaffold. This ability to interact with microtubules plays a role in membrane tubulation.

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