The domain within your query sequence starts at position 295 and ends at position 566; the E-value for the Dus domain shown below is 2e-60.

YLAPLTTCGNLPFRRICKRFGADVTCGEMAVCTNLLQGQMSEWALLKRHPCEDIFGVQLE
GAFPDTMTKCAELLNRTIDVDFVDINVGCPIDLVYKKGGGCALMNRSAKFQQIVRGVNEV
LDVPLTVKMRTGVQERVSLAHRLLPELRDWGVALVTLHGRSREQRYTRLADWPYIEQCAK
VASPMPLFGNGDILSFEDANCAMQTGVAGIMVARGALLKPWLFTEIKEQRHWDISSSERL
DILRDFTHYGLEHWGSDTQGVERTRRFLLEWL

Dus

Dus
PFAM accession number:PF01207
Interpro abstract (IPR001269):

Members of this family catalyse the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 (P53759) from Saccharomyces cerevisiae (Baker's yeast) acts on pre-tRNA-Phe, while Dus 2 (P53720) acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD [(PUBMED:12003496)]. Some family members may be targeted to the mitochondria and even have a role in mitochondria [(PUBMED:12003496)].

GO process:tRNA processing (GO:0008033), oxidation-reduction process (GO:0055114)
GO function:flavin adenine dinucleotide binding (GO:0050660), tRNA dihydrouridine synthase activity (GO:0017150)

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