The domain within your query sequence starts at position 43 and ends at position 204; the E-value for the Bcl-2_BAD domain shown below is 5e-93.

MFQIPEFEPSEQEDASATDRGLGPSLTEDQPGPYLAPGLLGSNIHQQGRAATNSHHGGAG
AMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSF
KGLPRPKSAGTATQMRQSAGWTRIIQSWWDRNLGKGGSTPSQ

Bcl-2_BAD

Bcl-2_BAD
PFAM accession number:PF10514
Interpro abstract (IPR018868):

BAD is a Bcl-2 homology domain 3 (BH3)-only pro-apoptotic member of the Bcl-2 protein family that is regulated by phosphorylation in response to survival factors [ (PUBMED:9372935) ]. Binding of BAD to mitochondria is thought to be exclusively mediated by its BH3 domain. Membrane localisation of BAD mediates membrane translocation of Bcl-XL. The C-terminal part of BAD is sufficient for membrane binding. There are two segments with differing lipid-binding preferences, LBD1 and LBD2, that are responsible for this binding: (i) LBD1 located in the proximity of the BH3 domain (amino acids 122-131) and (ii) LBD2, the putative C-terminal alpha-helix-5 [ (PUBMED:16226704) ]. Phosphorylation-regulated 14-3-3 protein binding may expose the cholesterol-preferring LBD1 and bury the LBD2, thereby mediating translocation of BAD to raft-like micro-domains [ (PUBMED:16603546) ].

GO process:apoptotic process (GO:0006915)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Bcl-2_BAD