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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 PRU01398


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU01398
General rule information [?]

Accession PRU01398
Dates 22-OCT-2024 (Created)
22-OCT-2024 (Last updated, Version 2)
Data class Domain;
Predictors PROSITE; PS52053; NEL
Name Novel E3 ligase (NEL) domain
Function The ~300 residue NEL domain bears a cysteine residue that mediates transfer of ubiquitin to substrates through the formation of a thioester intermediate, analogous to the structurally unrelated HECT domain in eukaryotes.
Scope(s) Bacteria
Pseudomonadota
Example(s) A0A0H2USC0;

Propagated annotation [?]

Comments [?]

case <FTTag:act_site>
PTMUbiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin.
end case
SIMILARITYBelongs to the LRR-containing bacterial E3 ligase family.

Keywords [?]


Gene Ontology [?]

GO:0005576; Cellular component:extracellular region
case <FTTag:act_site>
GO:0004842; Molecular function:ubiquitin-protein transferase activity

Features [?]

From: PS52053
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="NEL #"
ACT_SITE 89 89 /note="Glycyl thioester intermediate" act_site C

Additional information [?]

Size range 280-295 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 [?]