The domain within your query sequence starts at position 16 and ends at position 343; the E-value for the A_deaminase domain shown below is 3e-44.

QLPKVELHAHLNGSISSSTMKKLIAKKPHLNVHGHMTMIDKGKKRTLQECFQMFQVIHQL
TTSAEDILMVTKDVIKEFADDGVKYLELRSTPREENATGMTRKTYVESVLEGIKQCKQEN
LDIDVRYLMAIDRRGGPTIARETVELAKEFFLSTENTVLGLDLSGDPTIGQANDFLEPLL
EAKKAGLKLALHLAEIPNREKENQMLLSLLPDRIGHGTFLSASEAGALDQVDFVRQHQIP
LELCLTSNIKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATYLSQEYQLAAETFNLT
PFQVWDLSYESINYIFACDNTRSELRKR

A_deaminase

A_deaminase
PFAM accession number:PF00962
Interpro abstract (IPR001365):

Adenosine deaminase (EC 3.5.4.4) catalyzes the hydrolytic deamination of adenosine into inosine and AMP deaminase (EC 3.5.4.6) catalyzes the hydrolytic deamination of AMP into IMP. It has been shown [(PUBMED:1998686)] that these two enzymes share three regions of sequence similarities; these regions are centred on residues which are proposed to play an important role in the catalytic mechanism of these two enzymes.

This entry represents the main structural domain of adenosine deaminase and AMP deaminase proteins.

GO function:deaminase activity (GO:0019239)

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