SMART: Pfam domain LEM

The domain within your query sequence starts at position 74 and ends at position 112; the E-value for the LEM domain shown below is 6.6e-12.

LKLLNPDDLRKEVMKAGLKCGPITSTTRFIFEKKLAQAL

LEM

PFAM accession number:	PF03020
Interpro abstract (IPR003887):	The LEM (LAP2, emerin, MAN1) domain is a globular module of approximately 40 amino acids, which is mostly found in the nucleoplasmic portions of metazoan inner nuclear membrane proteins. The LEM domain has been shown to mediate binding to BAF (barrier-to-autointegration factor) and BAF-DNA complexes. BAF dimers bind to double-stranded DNA non-specifically and thereby bridge DNA molecules to form a large, discrete nucleoprotein complex [ (PUBMED:10671519) (PUBMED:11500367) ]. The resolution of the solution structure of the LEM domain reveals that it is composed of a three-residue N-terminal helical turn and two large parallel alpha helices interacting through a set of conserved hydrophobic amino acids. The two helices, which are connected by a long loop are oriented at an angle of ~45 degree [ (PUBMED:11500367) (PUBMED:11435115) ]. Proteins known to contain a LEM domain include: Vertebrate inner nuclear membrane protein MAN1. Vertebrate lamina-associated polypeptide 2 (LAP2) or thymopoietin. Mammalian emerin (EMD). In human, defects in EMD are a cause of X-linked Emery-Dreifuss muscular dystrophy (X-EDMD), an X-linked disorder, characterised by early contractures, muscle wasting and weakness and cardiomyopathy. Xenopus laevis Smad1 antagonistic effector (SANE). Drosophila melanogaster otefin (OTE). Caenorhabditis elegans W01G7.5 protein.

PFAM accession number:

PF03020

Interpro abstract (IPR003887):

The LEM (LAP2, emerin, MAN1) domain is a globular module of approximately 40 amino acids, which is mostly found in the nucleoplasmic portions of metazoan inner nuclear membrane proteins. The LEM domain has been shown to mediate binding to BAF (barrier-to-autointegration factor) and BAF-DNA complexes. BAF dimers bind to double-stranded DNA non-specifically and thereby bridge DNA molecules to form a large, discrete nucleoprotein complex [ (PUBMED:10671519) (PUBMED:11500367) ].

The resolution of the solution structure of the LEM domain reveals that it is composed of a three-residue N-terminal helical turn and two large parallel alpha helices interacting through a set of conserved hydrophobic amino acids. The two helices, which are connected by a long loop are oriented at an angle of ~45 degree [ (PUBMED:11500367) (PUBMED:11435115) ].

Proteins known to contain a LEM domain include:

Vertebrate inner nuclear membrane protein MAN1.
Vertebrate lamina-associated polypeptide 2 (LAP2) or thymopoietin.
Mammalian emerin (EMD). In human, defects in EMD are a cause of X-linked Emery-Dreifuss muscular dystrophy (X-EDMD), an X-linked disorder, characterised by early contractures, muscle wasting and weakness and cardiomyopathy.
Xenopus laevis Smad1 antagonistic effector (SANE).
Drosophila melanogaster otefin (OTE).
Caenorhabditis elegans W01G7.5 protein.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry LEM