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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

ProRule PRU01236


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU01236
General rule information [?]

Accession PRU01236
Dates 28-MAR-2019 (Created)
22-NOV-2019 (Last updated, Version 4)
Data class Domain;
Predictors PROSITE; PS51888; CLIP
Name Clip domain
Function Although the functions of clip domains are not completely clear, the clip domain in arthropods has been demonstrated to act in the regulation of proteinase activity, protein-protein interaction and bactericidal activities.
Scope(s) Eukaryota
Arthropoda
Example(s) Q9VB68;

Propagated annotation [?]

Comments [?]

DOMAINThe clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
SIMILARITYBelongs to the peptidase S1 family. CLIP subfamily.

Keywords [?]

case <FTTag:disulf>
Disulfide bond
end case

Features [?]

From: PS51888
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Clip #"
DISULFID 2 52 disulf C-x*-C
DISULFID 12 42 disulf C-x*-C
DISULFID 18 53 disulf C-x*-C

Additional information [?]

Size range 40-65 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

Copyright

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 [?]