The domain within your query sequence starts at position 394 and ends at position 485; the E-value for the Ant_C domain shown below is 7.4e-46.

VRWGDKGSTEEGARLEKAKNAVVMVPEEEIPIPSRPPRPRPTHQAPQTKWYTPIKGRLDA
LWALIMKQYDRVSLMRPQEGDEGRCINFSRVP

Ant_C

Ant_C
PFAM accession number:PF05586
Interpro abstract (IPR008399):

Anthrax is an acute disease in humans and animals, which is caused by the bacterium Bacillus anthracis. While the disease can be lethal, there are effective vaccines against anthrax, and some forms of the disease respond well to antibiotic treatment.

The anthrax toxin consists of the proteins protective antigen (PA), lethal factor (LF) and oedema factor (EF). The first step of toxin entry into host cells is the recognition by PA of a receptor on the surface of the target cell. The subsequent cleavage of receptor-bound PA enables EF and LF to bind and form a heptameric PA63 pre-pore, which triggers endocytosis. PA has been shown to bind to two cellular receptors, termed anthrax toxin receptor 1 (ANTXR1/TEM8) and 2 (ANTXR2). Both bind to PA with high affinity and are capable of mediating toxicity [(PUBMED:15243628), (PUBMED:15079089)], and both are type 1 membrane proteins that include an approximately 200-aa extracellular von Willebrand factor A (VWA) domain with a metal ion-dependent adhesion site (MIDAS) motif [(PUBMED:15079089)].

This region is found in the putatively cytoplasmic C terminus of the anthrax receptor.

GO component:integral component of membrane (GO:0016021)
GO function:signaling receptor activity (GO:0038023)

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