The domain within your query sequence starts at position 330 and ends at position 806; the E-value for the AMP-binding domain shown below is 4.3e-26.

LQLWGTTQPKAPCLTALDTAGKATCTLTYGKLWSRSLKLAYTLLNKLTSKNEPLLNPGDR
VALVFPNSDPVMFMVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVTLALTTD
ACQKGLPKAPTGEVATFKGWPPLAWLVIDGKHLTRPPKDWYPLAQDTGSRTAYIEYKTSK
EGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVI
TIPYALMKVNPLSWIQKVCSYKARAALVKSRDMHWSLLAQRGQRDVCLSSLRMLIVADGA
NPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDLGGPPPRKAVLSMNGL
SYGVIRVDTEEKLSVLTVQDVGQVMPGASVCVVKVDGAPYLCKTDEIGEICVNSVATGTA
YYGLLGITKNTFETVPVTADGVPVSDRPFTRTGLLGFIGPDNLVFVVGKLDGLMVVG

AMP-binding

AMP-binding
PFAM accession number:PF00501
Interpro abstract (IPR000873):

A number of prokaryotic and eukaryotic enzymes, which appear to act via an ATP-dependent covalent binding of AMP to their substrate, share a region of sequence similarity [ (PUBMED:2118102) (PUBMED:2911486) (PUBMED:2254270) ]. This region is a Ser/Thr/Gly-rich domain that is further characterised by a conserved Pro-Lys-Gly triplet. The family of enzymes includes luciferase, long chain fatty acid Co-A ligase, acetyl-CoA synthetase and various other closely-related synthetases [ (PUBMED:26473393) ].

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