The domain within your query sequence starts at position 22 and ends at position 484; the E-value for the Amidase domain shown below is 6e-129.
ELCKNCLSLIKKTKYLNAYITVSEEVALKQAEESEKRYKQGQSLGDLDGIPVAVKDNFST TGIETTCASNMLKGYVPPYNATVVQKLLDQGALLMGKTNLDEFAMGSGSTDGVFGPVRNP WTYSKQYRERSRQDAGDDSHWLITGGSSGGSAAAVAAFTCFAALGSDTGGSTRNPAAHCG IVGFKPSYGLVSRHGLIPLVNSMDVPGILTRCVDDTAIVLGTLAGHDPKDSTTVRNPAQP ASVPGGMDVSRLCIGIPKEYLVPELSSEVRSLWSQAADLFESEGAKVIEVSLPHTCYSIV CYHVLCTSEVASNMARFDGLQYGHRSGVDVSTEAMYAATRQEGFNDVVRGRILSGNFFLL KENYENYFVKAQKVRRLIVKDFVDVFESGVDVLLTPTTLTEAVPYLEFIKEDNRTRSAQD DIFTQAVNMAGLPAVSVPVALSNQGLPIGLQLIGRAFCDQQLL
Amidase |
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PFAM accession number: | PF01425 |
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Interpro abstract (IPR023631): | Amidase signature (AS) enzymes are a large group of hydrolytic enzymes that contain a conserved stretch of approximately 130 amino acids known as the AS sequence. They are widespread, being found in both prokaryotes and eukaryotes. AS enzymes catalyse the hydrolysis of amide bonds (CO-NH2), although the family has diverged widely with regard to substrate specificity and function. Nonetheless, these enzymes maintain a core alpha/beta/alpha structure, where the topologies of the N- and C-terminal halves are similar. AS enzymes characteristically have a highly conserved C-terminal region rich in serine and glycine residues, but devoid of aspartic acid and histidine residues, therefore they differ from classical serine hydrolases. These enzymes posses a unique, highly conserved Ser-Ser-Lys catalytic triad used for amide hydrolysis, although the catalytic mechanism for acyl-enzyme intermediate formation can differ between enzymes [ (PUBMED:15595822) ]. Examples of AS enzymes include:
The amidase signature enzymes consist structurally of a core domain that is covered by alpha-helices [ (PUBMED:12367528) ]. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Amidase