The domain within your query sequence starts at position 25 and ends at position 808; the E-value for the Prominin domain shown below is 3.6e-279.

AVTDDCGSLGRVEHLAFARVPRTRELAPLVRASGPLNSLYGTVRRFLSVVQLNPFPAELI
KTLLNDPSSVKTDEVVRYEAGYVVCAVIAGLYLLLVPITGLCFCCCRCRQRCGGRVKTEH
KAMACERGTLMIFLLLTTLVLLIGMVCAFATNQHTHSQTGPSVKAVPETLLSLRGLVSDV
PEELRAIAEQFSVPQKQVSKELDGVGENLGNVIHNRLKSTVYPVLASVHSLGQALQVSID
HLRALNTTSVELQEAQRHLEPPVQAHRERLLALLQDSWCHEENCKRVLSQAGALQLGADF
SQTPPVDDVLHRLKDVPETNFSSMVQEEKATFNNLPLLVQVQAVSVVKDVKKALAEQPEG
LRMLAQAFPGSEAASRWSQALEGLEQRSRPYLQEVQQYETYRWILGCVLCSAILLVVICN
LLGLSLGIWGLFAREDPSHSETKGEAGARLLMAGVAFSFLFAVPLILLVFVTFLVGGNVQ
TLVCRSWESGELYEFADTPGNLPPSMNLSYLLGLKKNISIVQAYRQCKAGAVLWKVLQLN
DSYDLDKHLDIKQYTHKIQQELQSFQVDLKELDLLSPTARQDLEALQRSGLEKIHYRGFL
VQIQKPVVNTDMWQLAQELEGLAQAQNDSLLRQQLREEARELRSLYQEKVVPQESLVTKL
NFSVKTLESLAPSLQVNTSDFLDSVTRLKGELPVQINHILRNATECFLTREMGYFSQYVT
WVRAEVTQRIATCQPFSTALDNGHVILCDMMADPWNAFWFCLGWCTFFLIPSIIFAVKTS
KYFR

Prominin

Prominin
PFAM accession number:PF05478
Interpro abstract (IPR008795): The prominins are an emerging family of proteins that, among the multispan membrane proteins, display a novel topology. Mouse and Homo sapiens prominin and (Mus musculus) prominin-like 1 (PROML1) are predicted to contain five membrane spanning domains, with an N-terminal domain exposed to the extracellular space followed by four, alternating small cytoplasmic and large extracellular, loops and a cytoplasmic C-terminal domain [(PUBMED:11467842)]. The exact function of prominin is unknown although in humans defects in PROM1, the gene coding for prominin, cause retinal degeneration [(PUBMED:10587575)].
GO component:integral component of membrane (GO:0016021)

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