The domain within your query sequence starts at position 3 and ends at position 75; the E-value for the Bcr-Abl_Oligo domain shown below is 1.2e-44.

DSVGFAEAWRAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTL
LAKEKKSYDRQRW

Bcr-Abl_Oligo

• PFAM accession number: PF09036
• Interpro abstract (IPR015123):

  This entry represents the oligomerisation domain of the breakpoint cluster region oncoprotein Bcr, and the Bcr/Abl (Abelson-leukemia-virus) fusion protein created by a reciprocal (9;22) fusion [ (PUBMED:17090304) ]. Brc displays serine/threonine protein kinase activity ( EC 2.7.11.1 ), acting as a GTPase-activating protein for RAC1 and CDC42. Brc promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them [ (PUBMED:15302586) ]. The Bcr/Abl fusion protein loses some of the regulatory function of Bcr with regards to small Rho-like GTPases with negative consequences on cell motility, in particular on the capacity to adhere to endothelial cells [ (PUBMED:17090304) ].

  The Bcr, Bcr/Abl oncoprotein oligomerisation domain consists of a short N-terminal helix (alpha-1), a flexible loop and a long C-terminal helix (alpha-2). Together these form an N-shaped structure, with the loop allowing the two helices to assume a parallel orientation. The monomeric domains associate into a dimer through the formation of an antiparallel coiled coil between the alpha-2 helices and domain swapping of two alpha-1 helices, where one alpha-1 helix swings back and packs against the alpha-2 helix from the second monomer. Two dimers then associate into a tetramer. The oligomerisation domain is essential for the oncogenicity of the Bcr-Abl protein [ (PUBMED:11780146) ].

• GO process: protein phosphorylation (GO:0006468), signal transduction (GO:0007165)
• GO function: protein serine/threonine kinase activity (GO:0004674), GTPase activator activity (GO:0005096)

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