The domain within your query sequence starts at position 228 and ends at position 473; the E-value for the Peptidase_M48 domain shown below is 5.5e-75.
PLPEGKLKQEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEY SVPNKDNQEESGMEARNEGEGDSEEVKAKVKNKKQGCKNEEVLAVLGHELGHWKLGHTVK NIIISQMNSFLCFFLFAVLIGRRELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCL TVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSTWHYSHPPLLERLQ ALKNAK
Peptidase_M48 |
---|
PFAM accession number: | PF01435 |
---|---|
Interpro abstract (IPR001915): | This entry represents the largely extracellular catalytic region of CAAX prenyl protease homologues such as Human FACE-1 protease. These are metallopeptidases, with the characteristic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds to form a deep groove/cleft into which the substrate can fit [ (PUBMED:23539602) (PUBMED:23539603) ]. This group of metallopeptidases belong to MEROPS peptidase family M48. Proteins with this domain are mostly described as probable protease htpX homologue ( EC 3.4.24 ) or CAAX prenyl protease 1, which proteolytically removes the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and Golgi, binding one zinc ion per subunit. |
GO process: | proteolysis (GO:0006508) |
GO function: | metalloendopeptidase activity (GO:0004222) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M48