SMART: Pfam domain Ceramidse_alk

The domain within your query sequence starts at position 586 and ends at position 753; the E-value for the Ceramidse_alk_C domain shown below is 8e-50.

FRDLAKAIATDTVANMSSGPEPPFFKNLIASLIPNIADRAPIGKHFGDVLQPAKPEYRVG
EVVEVIFVGANPKNSAENQTHQTFLTVEKYEDSVADWQIMYNDASWETRFYWHKGILGLS
NATIYWHIPDTAYPGIYRIRYFGHNRKQELLKPAVILAFEGISSPFEV

Ceramidse_alk_C

PFAM accession number:	PF17048
Interpro abstract (IPR031331):	This family represents the C-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 C-terminal tail of the enzyme is highly conserved across all species and may play a role in the interaction of the enzyme with the plasma membranes. The tail is also vital for the stabilisation of the enzyme as a whole [ (PUBMED:19088069) ].

PFAM accession number:

PF17048

Interpro abstract (IPR031331):

This family represents the C-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 C-terminal tail of the enzyme is highly conserved across all species and may play a role in the interaction of the enzyme with the plasma membranes. The tail is also vital for the stabilisation of the enzyme as a whole [ (PUBMED:19088069) ].

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