ProRule PRU01432
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PURL: https://purl.expasy.org/prosite/rule/PRU01432
General rule information
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| Accession | PRU01432 |
| Dates | 09-MAR-2026 (Created)
09-MAR-2026 (Last updated, Version ) |
| Data class | Domain; |
| Predictors |
PROSITE; PS52087; LNS2 |
Name | Lipin/Ned1/Smp2 (LNS2) domain |
| Function | The lipin/Ned1/Smp2 (LNS2) domain of 180 amino acids, originally characterized as the Mg(2+)-dependent catalytic domain of PA phosphatases (lipins), is catalytically inactive in Nir proteins and RdgBalpha that exhibit substitutions for a critical catalytic aspartate residue and another Mg(2+)-coordinating residue. Nevertheless, the LNS2 domain retains the ability to bind PA, with two conserved lysine residues shown to be essential for this interaction. |
| Scope(s) |
Eukaryota |
| Example(s) | Q5U2N3; |
Propagated annotation
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Comments
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| case <FTGroup:1> | |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; |
Keywords
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| Magnesium | |
| Metal-binding | |
| end case | |
Gene Ontology
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| GO:0000287; Molecular function:magnesium ion binding |
Features
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| From: PS52087 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="LNS2 #" | |||||||||
| MOTIF | 7 | 11 | /note="DXDXT motif" | D-x-D-x-T | ||||||||
| MOTIF | 18 | 22 | /note="LXXIL motif" | L-x(2)-I-L | ||||||||
| BINDING | 7 | 7 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
D | 1 | |||||||
| BINDING | 9 | 9 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
D | 1 | |||||||
| BINDING | 127 | 127 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
N | 1 | |||||||
Additional information
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| Size range | 161-197 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
Eukaryota [19] All [ 19 ]
- Retrieve set of proteins with 3D structure for this domain