The domain within your query sequence starts at position 32 and ends at position 110; the E-value for the SelP_N domain shown below is 2.1e-44.

QGQSSACYKAPEWYIGDQNPMLNSEGKVTVVALLQASUYLCLLQASRLEDLRIKLESQGY
FNISYIVVNHQGSPSQLKH

SelP_N

SelP_N
PFAM accession number:PF04592
Interpro abstract (IPR007671):

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 of SelP can exist independently of the C-terminal region. Zebrafish selenoprotein Pb (Q98SV0) lacks the C-terminal Sec-rich region, and a protein encoded by the rat SelP gene and lacking this region has also been reported [(PUBMED:11168591)]. The N-terminal region contains a conserved SecxxCys motif, which is similar to the CysxxCys found in thioredoxins. It is speculated that the N-terminal region may adopt a thioredoxin fold and catalyse redox reactions [(PUBMED:11168591)]. The N-terminal region also contains a His-rich region, which is thought to mediate heparin binding. Binding to heparan proteoglycans could account for the membrane binding properties of SelP [(PUBMED:10775431)].

The function of the bacterial members of this family is uncharacterised.

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