General rule information
[?]
Accession |
PRU01032 |
Dates |
20-AUG-2014 (Created) 22-NOV-2019 (Last updated, Version 4) |
Predictors |
PROSITE; PS51695; SEDOLISIN
|
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. |
Propagated annotation
[?]
case <FTGroup:2>
Cofactor |
Ca(2+) Note: Binds 1 Ca(2+) ion per subunit. |
end case
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
case <FTGroup:1>
end case
case <FTGroup:2>
end case
From: PS51695 |
Key
|
|
From
|
|
To
|
|
Description
|
|
Tag
|
|
Condition
|
|
FTGroup
|
DOMAIN
|
|
from
|
|
to
|
|
Peptidase S53 #
|
|
|
|
|
|
|
ACT_SITE
|
|
76
|
|
76
|
|
Charge relay system
|
|
|
|
E
|
|
1
|
ACT_SITE
|
|
80
|
|
80
|
|
Charge relay system
|
|
|
|
D
|
|
1
|
ACT_SITE
|
|
290
|
|
290
|
|
Charge relay system
|
|
|
|
S
|
|
1
|
METAL
|
|
332
|
|
332
|
|
Calcium
|
|
|
|
D
|
|
2
|
METAL
|
|
333
|
|
333
|
|
Calcium; via carbonyl oxygen
|
|
|
|
[IV]
|
|
2
|
METAL
|
|
354
|
|
354
|
|
Calcium; via carbonyl oxygen
|
|
|
|
G
|
|
2
|
METAL
|
|
356
|
|
356
|
|
Calcium
|
|
|
|
D
|
|
2
|
Additional information
[?]
Size range |
343-439 amino acids |
Related rules |
None |
Repeats |
1 |
Topology |
Undefined |
Example |
C5FHK0 (SED1_ARTOC) |
Scope |
Eukaryota
Bacteria; Proteobacteria |
Comments |
None |
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.
UniProtKB rule member sequences
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