AC PRU01032; DC Domain; TR PROSITE; PS51695; SEDOLISIN; 1; level=0 XX Names: Sedolisin domain Function: Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold ressembles that of subtilisin; however they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp (SED in single-letter notation), as well as the presence of an aspartic acid residue in the oxyanion hole. XX case CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 1 Ca(2+) ion per subunit.; end case XX case GO GO:0004252; F:serine-type endopeptidase activity end case case GO GO:0046872; F:metal ion binding end case XX case KW Hydrolase KW Protease KW Serine protease end case case KW Calcium KW Metal-binding end case XX FT From: PS51695 FT DOMAIN from..to FT /note="Peptidase S53 #" FT ACT_SITE 76 FT /note="Charge relay system" FT Group: 1; Condition: E FT ACT_SITE 80 FT /note="Charge relay system" FT Group: 1; Condition: D FT ACT_SITE 290 FT /note="Charge relay system" FT Group: 1; Condition: S FT BINDING 332 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: D FT BINDING 333 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: [IV] FT BINDING 354 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: G FT BINDING 356 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: D XX Chop: Nter=0; Cter=0; Size: 343-439; Related: None; Repeats: 1; Topology: Undefined; Example: C5FHK0; Scope: Eukaryota Bacteria; Pseudomonadota Comments: None; XX # Revision 1.7 2023/01/26 //