The domain within your query sequence starts at position 430 and ends at position 884; the E-value for the PigN domain shown below is 1.5e-141.

RGLSYYHTYDRLFLGINVAVGFVGWMSYTSLLIIKSHSNIPKGTRKEGKKPHCLLLYSFI
ATGVLVACFLMIQACPWTYYVYCLLPVPIWYAVLREHEVIQDLVESLLTFPRSHFVAYLL
VFTLGIEVLVLSFFYRYMLTAGLIVFAGWPFLTQLWTRAKITFLSWAFFSLLLAVFPLMP
VVGRKPNLSLVMGAGFLVLLLSLAVVTTLGKRNIKLVKGELLVLLLQMLSTVLSMYVVYS
THHSLLKKEGLPLMNQIVSWATLASSLVAPLLSSTALSQRLASILLSLMSTYLLLSTGYE
ALFPLVLSCLMFVWIQVEQETLQQPGVSCKQKLTSIQFTCDTDIAQFRQLCPDDIRRAFF
LVFFLLTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFVLVMCAFEAV
QITTQLSSKGLFLVVLIISDIMALHFFFLVKDSGS

PigN

 PigN
PFAM accession number:PF04987
Interpro abstract (IPR017852):

This entry represents the C-terminal region of GPI ethanolamine phosphate transferase 1 enzymes, including the yeast enzyme MCD4 and the mammalian homolgoue PIG-N (also known as phosphatidylinositolglycan class N) [ (PUBMED:10574991) (PUBMED:10069808) ]. These enzymes are multi-pass endoplasmic reticulum membrane proteins involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. These enzymes transfer ethanolamine phosphate to the first alpha-1,4-linked mannose of the GPI precursor of the GPI-anchor. Ethanolamine phosphate on the alpha-1,4-linked mannose is essential for further mannosylation by GPI10 and is necessary for an efficient recognition of GPI lipids and GPI proteins by the GPI transamidase, for the efficient transport of GPI anchored proteins from endoplasmic reticulum to Golgi and for the physiological incorporation of ceramides into GPI anchors by lipid remodeling. MCD4 is also involved in non-mitochondrial ATP movements across the membrane and participates in Golgi and endoplasmic reticulum function, and is required for the incorporation of BGL2 into the cell wall.

GO process:GPI anchor biosynthetic process (GO:0006506)
GO component:endoplasmic reticulum membrane (GO:0005789)
GO function:transferase activity (GO:0016740)

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