The domain within your query sequence starts at position 34 and ends at position 147; the E-value for the DUF498 domain shown below is 9.4e-28.

IASLSWGQMKVQGSTLTYKDCKVWPGGSRAWDWRETGTEHSPGVQPADVKEVAEKGVQTL
VIGRGMSEALKVPPSTVEYLEKQGIDVRVLQTEQAVKEYNALVAQGVRVGGVFH

DUF498

DUF498
PFAM accession number:PF04430
Interpro abstract (IPR007523):

This entry includes NDUFAF3, an essential factor for the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) [ (PUBMED:19463981) ], and the Mth938 domain-containing protein [ (PUBMED:22279136) ]. The crystal structure of NDUFAF3 revealed a 3-layer beta+alpha/beta/alpha topology [ (PUBMED:11746696) ].

NADH:ubiquinone oxidoreductase (complex I) ( EC 1.6.5.3 ) is a respiratory-chain enzyme that catalyses the transfer of two electrons from NADH to ubiquinone in a reaction that is associated with proton translocation across the membrane (NADH + ubiquinone = NAD+ + ubiquinol) [ (PUBMED:1470679) ]. Complex I is a major source of reactive oxygen species (ROS) that are predominantly formed by electron transfer from FMNH(2). Complex I is found in bacteria, cyanobacteria (as a NADH-plastoquinone oxidoreductase), archaea [ (PUBMED:10940377) ], mitochondria, and in the hydrogenosome, a mitochondria-derived organelle. In general, the bacterial complex consists of 14 different subunits, while the mitochondrial complex contains homologues to these subunits in addition to approximately 31 additional proteins [ (PUBMED:18394423) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry DUF498