The domain within your query sequence starts at position 78 and ends at position 584; the E-value for the Ceramidase_alk domain shown below is 1.4e-222.

YYIGVGRADCTGQVSDINLMGYGKNGQNARGLLTRLFSRAFILADPDGSNRMAFVSVELC
MISQRLRLEVLKRLESKYGSLYRRDNVILSAIHTHSGPAGFFQYTLYILASEGFSNRTFQ
YIVSGIMKSIDIAHTNLKPGKIFINKGNVANVQINRSPSSYLLNPQSERARYSSNTDKEM
LVLKLVDLNGEDLGLISWFAIHPVSMNNSNHFVNSDNMGYAAYLFEQEKNKGYLPGQGPF
VAGFASSNLGDVSPNILGPHCVNTGESCDNDKSTCPNGGPSMCMASGPGQDMFESTHIIG
RIIYQKAKELYASASQEVTGPVLAAHQWVNMTDVSVQLNATHTVKTCKPALGYSFAAGTI
DGVSGLNITQGTTEGDPFWDTLRDQLLGKPSEEIVECQKPKPILLHSGELTIPHPWQPDI
VDVQIVTVGSLAIAAIPGELTTMSGRRFREAIKKEFALYGMKDMTVVIAGLSNVYTHYIT
TYEEYQAQRYEAASTIYGPHTLSAYIQ

Ceramidase_alk

Ceramidase_alk
PFAM accession number:PF04734
Interpro abstract (IPR031329): This entry represents the N-terminal domain of a group of neutral/alkaline ceramidases found in both bacteria and eukaryotes [(PUBMED:10753931), (PUBMED:10781606), (PUBMED:10593963)]. The EC classification is (EC 3.5.1.23). The enzyme hydrolyses ceramide to generate sphingosine and fatty acid. The enzyme plays a regulatory role in a variety of physiological events in eukaryotes and also functions as an exotoxin in particular bacteria. This N-terminal domain carries two metal-binding sites, the first for Zn2+ residing within the domain, and the second, for Mg2+/Ca2+ lying at the interface between the two domains [(PUBMED:19088069)].

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