The domain within your query sequence starts at position 100 and ends at position 380; the E-value for the Exostosin domain shown below is 1.4e-57.

PKNKIKVYIYPLKKYVDDAGVPVSSAISREYNELLTAISDSDYYTDDINRACLFVPSIDV
LNQNPLRIKETAQALAQLSRWDRGTNHLLFNMLPGAPPDYNTALDVPRDRALLAGGGFST
WTYRQGYDVSIPVFSPLSAEMALPEKAPGPRRYFLLSSQMAIHPEYREELEALQAKHQES
VLVLDKCTNLSEGVLSVRKRCHQHQVFDYPQVLQEATFCTVLRGARLGQAVLSDVLQAGC
VPVVIADSYILPFSEVLDWKRASVVVPEEKMSDVYSILQNI

Exostosin

Exostosin
PFAM accession number:PF03016
Interpro abstract (IPR004263):

There are five identified human EXT family proteins (EXT1, EXT2, EXTL1, EXTL2 and EXTL3), which are members of the hereditary multiple exostoses family of tumor suppressors [(PUBMED:17237233)]. They are glycosyltransferases required for the biosynthesis of heparan sulfate. Hereditary multiple exostoses (EXT) is an autosomal dominant disorder that is characterised by the appearance of multiple outgrowths of the long bones (exostoses) at their epiphyses [(PUBMED:9473480)]. Mutations in two homologous genes, EXT1 and EXT2, are responsible for the EXT syndrome. The human and mouse EXT genes have at least two homologues in the invertebrate Caenorhabditis elegans, indicating that they do not function exclusively as regulators of bone growth. EXT1 and EXT2 have both been shown to encode glycosyltransferases involved in the chain elongation step of heparan sulphate biosynthesis [(PUBMED:9756849)].

This entry also includes Arabidopsis Xyloglucan galactosyltransferase KATAMARI1 [(PUBMED:12837954)] and Drosophila melanogaster EXT homologues [(PUBMED:14998928)].

GO process:protein glycosylation (GO:0006486)
GO function:transferase activity, transferring glycosyl groups (GO:0016757)

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