AC   PRU01432;
DC   Domain;
TR   PROSITE; PS52087; LNS2; 1; level=0
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Names: 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.
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case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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GO   GO:0000287; F:magnesium ion binding
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KW   Magnesium
KW   Metal-binding
end case
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FT   From: PS52087
FT   DOMAIN          from..to
FT                   /note="LNS2 #"
FT   MOTIF           7..11
FT                   /note="DXDXT motif"
FT   Condition: D-x-D-x-T
FT   MOTIF           18..22
FT                   /note="LXXIL motif"
FT   Condition: L-x(2)-I-L
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: N
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Chop: Nter=0; Cter=0;
Size: 161-197;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5U2N3;
Scope:
 Eukaryota
Comments: None;
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# Version: 1
# Last updated date: 2026-03-09
# Created date: 2026-03-09
//