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

• 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