Preferred Label : PR-SET Domains;
MeSH definition : Highly conserved protein domains of approximately 130 to 140 amino acids. The SET
domain was first identified in the Drosophila proteins (S)u(var)3-9, (E)nhancer-of-zeste
and (T)rithorax and occurs in other proteins with a variety of functions, including
histone-lysine N-methyltransferases. Structurally, it consists of BETA-SHEETS interspersed
among loops and turns that result in an L shape. The most conserved motifs are a stretch
at the C-terminal that contains a strictly conserved tyrosine residue and an adjacent
loop that the C-terminal segment passes through to form a knot. These motifs and especially
the tyrosine residue are essential for S-ADENOSYLMETHIONINE binding and catalysis.
The PR domain has high homology to the catalytic region of the SET domain and occurs
at the N-terminal of PRDM proteins such as PRDM1 PROTEIN.;
MeSH synonym : Domain, PR-SET; Domains, PR-SET; PR SET Domains; PR-SET Domain;
DeCS synonym : SET Domain; PR Domain;
MeSH hyponym : Domain, SET; Domains, SET; SET Domains; Domain, PR; Domains, PR; PR Domains;
Origin ID : D000074463;
UMLS CUI : C4505240;
Allowable qualifiers
- Automatic exact mappings (from CISMeF team)
- Record concept(s)
- See also
- Semantic type(s)
Highly conserved protein domains of approximately 130 to 140 amino acids. The SET
domain was first identified in the Drosophila proteins (S)u(var)3-9, (E)nhancer-of-zeste
and (T)rithorax and occurs in other proteins with a variety of functions, including
histone-lysine N-methyltransferases. Structurally, it consists of BETA-SHEETS interspersed
among loops and turns that result in an L shape. The most conserved motifs are a stretch
at the C-terminal that contains a strictly conserved tyrosine residue and an adjacent
loop that the C-terminal segment passes through to form a knot. These motifs and especially
the tyrosine residue are essential for S-ADENOSYLMETHIONINE binding and catalysis.
The PR domain has high homology to the catalytic region of the SET domain and occurs
at the N-terminal of PRDM proteins such as PRDM1 PROTEIN.
