The domain within your query sequence starts at position 32 and ends at position 215; the E-value for the N_Asn_amidohyd domain shown below is 1.4e-82.

LLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLT
HCDGSDTKAEVPLIMSSIKSFSEHAECGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDKQD
DDIHLVTLCVTELNDREENENHFPIIYGIAVNIKTAEIYRASFQDRGPEEQLRAARALAG
GPSL

N_Asn_amidohyd

N_Asn_amidohyd
PFAM accession number:PF14736
Interpro abstract (IPR026750): Protein N-terminal asparagine amidohydrolase (NTAN1) acts on the side-chain deamidation of N-terminal asparagine residues to aspartate. It is required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. NTAN1 does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position [(PUBMED:8089117), (PUBMED:7814382)].
GO function:protein-N-terminal asparagine amidohydrolase activity (GO:0008418)

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