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Descriptor English: PR-SET Domains
Descriptor Spanish: Dominios PR-SET
Descriptor dominios PR-SET
Entry term(s) dominio PR
dominio PR-SET
dominio SET
dominios PR
dominios SET
Scope note: Dominios de proteínas altamente conservados de unos 130 a 140 aminoácidos. El dominio SET se identificó por primera vez en las proteínas de Drosophila (S)u(var)3-9, (E)nhancer-of-zeste y (T)rithorax y se encuentra también en otras proteínas con diversas funciones como la histona-lisina N-metiltransferasa. Constan de LÁMINAS BETA intercaladas entre bucles y giros que resultan en una forma de L. Los motivos más conservados son un tramo en el extremo C-terminal que contiene un residuo de tirosina estrictamente conservado y un bucle adyacente por el que pasa el segmento C-terminal formando un nudo. Estos motivos, y especialmente el residuo de tirosina, son esenciales para la unión y catálisis de la S-ADENOSILMETIONINA. El dominio PR tiene una alta homología con la región catalítica del dominio SET y se encuentra en el extremo N-terminal de las proteínas PRDM como la PROTEÍNA PRDM1.
Descriptor Portuguese: Domínios PR-SET
Descriptor French: Domaines PR-SET
Entry term(s): Domain, PR
Domain, PR-SET
Domain, SET
Domains, PR
Domains, PR-SET
Domains, SET
PR Domain
PR Domains
PR SET Domains
PR-SET Domain
SET Domain
SET Domains
Tree number(s): G02.111.570.820.709.275.750.477
RDF Unique Identifier: https://id.nlm.nih.gov/mesh/D000074463
Scope note: 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.
Allowable Qualifiers: DE drug effects
GE genetics
IM immunology
PH physiology
RE radiation effects
Previous Indexing: Amino Acid Sequence (1996-2017)
Histone-Lysine N-Methyltransferase (1996-2017)
Public MeSH Note: 2018
History Note: 2018
DeCS ID: 57255
Unique ID: D000074463
Documents indexed in the Virtual Health Library (VHL): Click here to access the VHL documents
Date Established: 2018/01/01
Date of Entry: 2017/07/11
Revision Date: 2017/04/05
PR-SET Domains - Preferred
Concept UI M000626718
Scope note 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.
Preferred term PR-SET Domains
Entry term(s) Domain, PR-SET
Domains, PR-SET
PR SET Domains
PR-SET Domain
SET Domain - Narrower
Concept UI M000626719
Preferred term SET Domain
Entry term(s) Domain, SET
Domains, SET
SET Domains
PR Domain - Narrower
Concept UI M000626720
Preferred term PR Domain
Entry term(s) Domain, PR
Domains, PR
PR Domains



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