AC   PRU00204;
DC   Domain;
TR   PROSITE; PS50104; TIR; 1; level=0
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Names: 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.
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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>
DE   + AltName: Full=Probable NAD(+) hydrolase;
DE            EC=3.2.2.6;
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CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC         Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC   -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC       Self-association of TIR domains is required for NADase activity.
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KW   NAD
KW   Hydrolase
end case
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FT   From: PS50104
FT   DOMAIN          from..to
FT                   /note="TIR #"
FT   ACT_SITE        77
FT   Condition: 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>
FT   BINDING         10..11
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   BINDING         41
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: E
end case
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Chop: Nter=0; Cter=0;
Size: 125-180;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q6SZW1;
Scope:
 Eukaryota
Comments: None
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# Revision 1.11 2022/11/19
//