Phenomena and Processes

PR-SET Domains

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.

National Library of MedicineMedical Subject Headings2026

Structured Summary

Abstract

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.

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Synonyms

12 entry terms
  • Domain, PR-SET
  • Domains, PR-SET
  • PR SET Domains
  • PR-SET Domain
  • PR Domain
  • SET Domain
  • Domain, PR
  • Domain, SET
  • Domains, PR
  • Domains, SET
  • PR Domains
  • SET Domains

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Aspects Covered

5 allowable subheadings

Indexed with the subheadings drug effects, genetics, immunology, physiology, radiation effects.

MeSH Record

History Note

2018

MeSH Record

Previous Indexing

  • Amino Acid Sequence (1996-2017)
  • Histone-Lysine N-Methyltransferase (1996-2017)

MeSH Hierarchy

Tree Number

  1. G02.111.570.820w.709.275.750w.477w

AMA Style

References

  1. National Library of Medicine. PR-SET Domains. Medical Subject Headings (MeSH). 2026. Unique ID D000074463. http://id.nlm.nih.gov/mesh/2026/D000074463
  2. PR-SET Domains. In: Wikipedia. https://en.wikipedia.org/wiki/SET_domain
  3. PR-SET Domains. In: Wikidata. https://www.wikidata.org/wiki/Q24770667