The domain within your query sequence starts at position 43 and ends at position 202; the E-value for the Mesd domain shown below is 4.5e-85.

KKDIRDYNDADMARLLEQWEKDDDIEEGDLPEHKRPSAPIDFSKLDPGKPESILKMTKKG
KTLMMFVTVSGNPTEKETEEITSLWQGSLFNANYDVQRFIVGSDRAIFMLRDGSYAWEIK
DFLVSQDRCAEVTLEGQMYPGKGGGSKEKNKTKPEKAKKK

Mesd

Mesd
PFAM accession number:PF10185
Interpro abstract (IPR019330):

LRP chaperone MESD (also known as mesoderm development candidate 2) represents a set of highly conserved proteins found from nematodes to humans. It is a chaperone that specifically assists with the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). It also acts as a modulator of the Wnt pathway, since some LDLRs are coreceptors for the canonical Wnt pathway and is essential for specification of embryonic polarity and mesoderm induction [ (PUBMED:12581525) ]. The Drosophila homologue, known as boca, is an endoplasmic reticulum protein required for wingless signaling and trafficking of LDL receptor family members [ (PUBMED:12581524) ].

The final C-terminal residues, KEDL, are the endoplasmic reticulum retention sequence as it is an ER protein specifically required for the intracellular trafficking of members of the low-density lipoprotein family of receptors (LDLRs) [ (PUBMED:12581524) ]. The N- and C-terminal sequences are predicted to adopt a random coil conformation, with the exception of an isolated predicted helix within the N-terminal region, The central folded domain flanked by natively unstructured regions is the necessary structure for facilitating maturation of LRP6 (Low-Density Lipoprotein Receptor-Related Protein 6 Maturation) [ (PUBMED:17488095) ].

GO process:protein folding (GO:0006457)

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