SMART: Pfam domain CBAH

The domain within your query sequence starts at position 131 and ends at position 362; the E-value for the CBAH domain shown below is 9e-11.

CTSIVAQDSQGHIYHGRNLDYPFGKILRKLTANVQFIKNGQIAFTGTTFVGYVGLWTGQS
PHKFTISGDERDKGWWWENMIAALSLGHSPISWLIRKTLSESESFEAAVYTLAKTPLIAD
VYYIVGGTSPKEGVVITRDRGGPADIWPLDPLNGEWFRVETNYDHWKPAPKVDDRRTPAI
KALNATGQAHLNLETLFQVLSLFPVYNNYTIYTTVMSAAEPDKYLTMIRNPS

CBAH

PFAM accession number:	PF02275
Interpro abstract (IPR029132):	This domain can be found in several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) ( EC 3.5.1.24 ), penicillin acylase ( EC 3.5.1.11 ) and acid ceramidase ( EC 3.5.1.23 ). This domain is also found at the C terminus of acid ceramidase (AC) and N-acylethanolamine-hydrolysing acid amidase (NAAA) [ (PUBMED:15655246) ]. AC and NAAA can be cleaved into two chains: alpha and beta. This domain represent the alpha subunit (chain).

PFAM accession number:

PF02275

Interpro abstract (IPR029132):

This domain can be found in several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) ( EC 3.5.1.24 ), penicillin acylase ( EC 3.5.1.11 ) and acid ceramidase ( EC 3.5.1.23 ). This domain is also found at the C terminus of acid ceramidase (AC) and N-acylethanolamine-hydrolysing acid amidase (NAAA) [ (PUBMED:15655246) ]. AC and NAAA can be cleaved into two chains: alpha and beta. This domain represent the alpha subunit (chain).

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