The domain within your query sequence starts at position 2 and ends at position 472; the E-value for the RPE65 domain shown below is 4.9e-117.

EIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFS
IRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFT
DNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNV
LNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGV
TENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYT
DPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAV
PLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYI
FAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDV

RPE65

RPE65
PFAM accession number:PF03055
Interpro abstract (IPR004294):

Carotenoids such as beta-carotene, lycopene, lutein and beta-cryptoxanthine are produced in plants and certain bacteria, algae and fungi, where they function as accessory photosynthetic pigments and as scavengers of oxygen radicals for photoprotection. They are also essential dietary nutrients in animals. Carotenoid oxygenases cleave a variety of carotenoids into a range of biologically important products, including apocarotenoids in plants that function as hormones, pigments, flavours, floral scents and defence compounds, and retinoids in animals that function as vitamins, visual pigments and signalling molecules [(PUBMED:14704328)]. Examples of carotenoid oxygenases include:

  • Beta-carotene-15,15'-monooxygenase (BCDO1; EC 1.14.99.36) from animals, which cleaves beta-carotene symmetrically at the central double bond to yield two molecules of retinal [(PUBMED:14704328)].
  • Beta-carotene-9',10'-dioxygenase (BCDO2) from animals, which cleaves beta-carotene asymmetrically to apo-10'-beta-carotenal and beta-ionone, the latter being converted to retinoic acid. Lycopene is also oxidatively cleaved [(PUBMED:14704328)].
  • 9-cis-epoxycarotenoid dioxygenase from plants, which cleaves 9-cis xanthophylls to xanthoxin, a precursor of the hormone abscisic acid [(PUBMED:12834401)].
  • Apocarotenoid-15,15'-oxygenase from bacteria and cyanobacteria, which converts beta-apocarotenals rather than beta-carotene into retinal. This protein has a seven-bladed beta-propeller structure with four hisitidines that hold the iron active centre [(PUBMED:15821095)].
  • Retinal pigment RPE65 from animals, which in its soluble form binds all-trans retinol, and in its membrane-bound form binds all-trans retinyl esters. RPE65 is important for the production of 11-cis retinal during visual pigment regeneration [(PUBMED:14532273)].

GO process:oxidation-reduction process (GO:0055114)
GO function:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (GO:0016702)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry RPE65