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ProRule PRU00204


General rule information [?]

Accession PRU00204
Dates 12-DEC-2003 (Created)
19-NOV-2022 (Last updated, Version 11)
Data class Domain;
Predictors PROSITE; PS50104; TIR
Name TIR
Function The TIR domain has been defined as a scaffold that promotes assembly of signaling complexes via protein-protein interactions. However, the scaffolding function may be a a recent adaptation. The primordial function of the TIR domain is a self-association-dependent nicotinamide dinucleotide (NAD(+))-cleaving enzyme (NADase) activity that cleaves NAD(+) into nicotinamide (Nam) and ADP-ribose (ADPR), cyclic ADPR (cADPR) or variant cADPR (v-cADPR), with catalytic cleavage executed by a conserved glutamic acid.
Scope(s) Eukaryota
Example(s) Q6SZW1 (SARM1_HUMAN);

Propagated annotation [?]

Identifier, protein and gene names [?]

case <Feature:PS50104:6=F> and <Feature:PS50104:10=R> and <Feature:PS50104:36=D> and <Feature:PS50104:50=L> and <Feature:PS50104:73=W> and <Feature:PS50104:77=E>
Protein name + AltName: Full=Probable NAD(+) hydrolase;
                 EC=3.2.2.6;

Comments [?]

CATALYTIC ACTIVITY Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
DOMAINThe TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.

Keywords [?]

NAD
Hydrolase
end case

Features [?]

From: PS50104
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="TIR #"
ACT_SITE 77 77 E
case <Feature:PS50104:6=F> and <Feature:PS50104:10=R> and <Feature:PS50104:36=D> and <Feature:PS50104:50=L> and <Feature:PS50104:73=W>
BINDING 10 11 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
BINDING 41 41 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
E
end case

Additional information [?]

Size range 125-180 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.



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UniProtKB rule member sequences [?]