The domain within your query sequence starts at position 4 and ends at position 389; the E-value for the LuxC domain shown below is 9.8e-11.

ISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEE
VAHVLDEIDFTIKGLSDWAEDEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQ
PMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYPVIKGGVPETTELLKEKFDH
IMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQT
CVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKKV
AHGGTWDQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLA
LYVFSNNDKVIKKMIAETSSGGVTAN

LuxC

LuxC
PFAM accession number:PF05893
Interpro abstract (IPR008670):

This family consists of several bacterial Acyl-CoA reductase (also known as long-chain-fatty-acyl-CoA reductase) LuxC proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalysed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components [ (PUBMED:9128139) (PUBMED:2030669) ].

GO process:bioluminescence (GO:0008218), oxidation-reduction process (GO:0055114)
GO function:acyl-CoA dehydrogenase activity (GO:0003995)

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