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annotation rule: PRU00204

General rule information [?]

Accession PRU00204
Dates 12-DEC-2003 (Created)
28-NOV-2019 (Last updated, Version 8)
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.

Propagated annotation [?]


Description [?]

case <FTTag:act_site>
+ AltName: Full=Probable NAD(+) hydrolase; EC 3.2.2.6;

Comments [?]

Catalytic activity RHEA:16301: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
EC 3.2.2.6
PhysiologicalDirection=left-to-right (RHEA:16302)
Domain The 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       TIR #        
ACT_SITE     77     77           act_site   E  
case <FTTag:NAD_bind>
NP_BIND     10     11       NAD        
end case

case <FTTag:act_site>
BINDING     41     41       NAD   NAD_bind   E  
end case


Additional information [?]

Size range 125-180 amino acids
Related rules None
Repeats 1
Topology Undefined
Example Q6SZW1 (SARM1_HUMAN)
Scope
Eukaryota

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 [?]