The domain within your query sequence starts at position 39 and ends at position 126; the E-value for the SCAN domain shown below is 1.1e-18.

QLNFSPSNNGCWATQELQSLWKMFNSWLQPEKQTKEQMISQLVLEQFLLTGHCKDKYALT
EKWKASGSDMRRFMESLTDECLKPPVMV

SCAN

SCAN
PFAM accession number:PF02023
Interpro abstract (IPR003309):

A number of C2H2-zinc finger proteins contain a highly conserved N-terminal motif termed the SCAN (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) domain. The SCAN domain has been shown to be able to mediate homo- and hetero-oligomerisation [ (PUBMED:10567577) ]. These proteins can either activate or repress transcription, although isolated recombinant SCAN domains do not modulate significantly the transcription [ (PUBMED:8065901) (PUBMED:7673192) ]. In addition to these zinc finger transcription factors, an isolated SCAN domain without adjacent zinc finger motifs has been identified in some proteins [ (PUBMED:10393183) (PUBMED:10747874) ]. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein [ (PUBMED:15629724) ].

The SCAN domain is enriched in hydrophobic and negatively charged residues with a L-X(6)-L motif at its core. This core is flanked by A, E, L, M, H and C residues that are frequently found in alpha-helices [ (PUBMED:7673192) ]. Predictions of the secondary structure of the domain suggest the presence of at least three alpha-helices that are separated from one another by short looped regions bounded by proline residues [ (PUBMED:10567577) ]. It has been shown to be a selective oligomerization domain that mediates homotypic and heterotypic interactions between SCAN box containing proteins [ (PUBMED:10747874) (PUBMED:10567577) ].

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