The domain within your query sequence starts at position 51 and ends at position 191; the E-value for the Myelin_MBP domain shown below is 2.7e-47.

LATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKVPWLKQSRSPLPSHAR
SRPGLCHMYKDSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGL
SLSRFSWGGRDSRSGSPMARR

Myelin_MBP

Myelin_MBP
PFAM accession number:PF01669
Interpro abstract (IPR000548):

The myelin sheath is a multi-layered membrane, unique to the nervous system, that functions as an insulator to greatly increase the velocity of axonal impulse conduction [ (PUBMED:2435734) ]. Myelin basic protein (MBP) [ (PUBMED:1710177) (PUBMED:1710279) ] is a hydrophilic protein that may function to maintain the correct structure of myelin, interacting with the lipids in the myelin membrane by electrostatic and hydrophobic interactions. In mammals various forms of MBP exist which are produced by the alternative splicing of a single gene; these forms differ by the presence or the absence of short (10 to 20 residues) peptides in various internal locations in the sequence. The major form of MBP is generally a protein of about 18.5 Kd (170 residues). MBP is the target of many post-translational modifications: it is N-terminally acetylated, methylated on an arginine residue, phosphorylated by various serine/threonine protein-kinases, and deamidated on some glutamine residues.

GO function:structural constituent of myelin sheath (GO:0019911)

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