The domain within your query sequence starts at position 249 and ends at position 380; the E-value for the SelP_C domain shown below is 2.6e-78.

GQHRQGHLESUDTTASEGLHLSLAQRKLURRGCINQLLCKLSKESEAAPSSCCCHCRHLI
FEKSGSAIAUQCAENLPSLCSUQGLFAEEKVTESCQCRSPPAAUQNQPMNPMEANPNUSU
DNQTRKUKUHSN

SelP_C

SelP_C
PFAM accession number:PF04593
Interpro abstract (IPR007672): SelP is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues, and accounts for more than 50% of the selenium content of rat and human plasma [(PUBMED:10775431)]. It is thought to be glycosylated [(PUBMED:11168591)]. SelP may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity [(PUBMED:10775431)]. The high selenium content of SelP suggests that it may be involved in selenium intercellular transport or storage [(PUBMED:11168591)]. The promoter structure of bovine SelP suggests that it may be involved in countering heavy metal intoxication, and may also have a developmental function [(PUBMED:9358058)]. The N-terminal region always contains one Sec residue, and this is separated from the C-terminal region (9-16 sec residues) by a histidine-rich sequence [(PUBMED:11168591)]. The large number of Sec residues in the C-terminal portion of SelP suggests that it may be involved in selenium transport or storage. However, it is also possible that this region has a redox function [(PUBMED:11168591)].

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