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.
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.
ProRule PRU00204
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00204
General rule information
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| Accession | PRU00204 |
| Dates | 12-DEC-2003 (Created)
03-SEP-2024 (Last updated, Version 13) |
| 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; |
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=NAD(+) + H2O = ADP-D-ribose + nicotinamide + H(+); 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" |
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| 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