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