ProRule PRU01032

General rule information [?]

Accession PRU01032
Dates 20-AUG-2014 (Created)
26-JAN-2023 (Last updated, Version 7)
Data class Domain;
Predictors PROSITE; PS51695; SEDOLISIN
Name 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.
Scope(s) Eukaryota
Example(s) C5FHK0 (SED1_ARTOC);

Propagated annotation [?]

Comments [?]

case <FTGroup:2>
COFACTOR Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.;
end case

Keywords [?]

case <FTGroup:1>
Serine protease
end case
case <FTGroup:2>
end case

Gene Ontology [?]

case <FTGroup:1>
GO:0004252; Molecular function:serine-type endopeptidase activity
end case
case <FTGroup:2>
GO:0046872; Molecular function:metal ion binding
end case

Features [?]

From: PS51695
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Peptidase S53 #"
ACT_SITE 76 76 /note="Charge relay system" E 1
ACT_SITE 80 80 /note="Charge relay system" D 1
ACT_SITE 290 290 /note="Charge relay system" S 1
BINDING 332 332 /ligand="Ca(2+)"
D 2
BINDING 333 333 /ligand="Ca(2+)"
[IV] 2
BINDING 354 354 /ligand="Ca(2+)"
G 2
BINDING 356 356 /ligand="Ca(2+)"
D 2

Additional information [?]

Size range 343-439 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined


PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

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UniProtKB rule member sequences [?]