ProRule PRU00204
General rule information
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| 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
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Identifier, protein and gene names
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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> | |
| Protein name | + AltName: Full=Probable NAD(+) hydrolase; EC=3.2.2.6; |
Comments
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| 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; |
| DOMAIN | The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity. |
Keywords
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Features
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| 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
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| Size range | 125-180 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
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
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- UniProtKB/Swiss-Prot sets
Archaea [2] Bacteria [20] Eukaryota [190] All [ 212 ]
- Retrieve set of proteins with 3D structure for this domain