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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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Amos Bairoch

PROSITE documentation PDOC50815
HORMA domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC50815

Description

The HORMA domain (for HOP1, REV7 and MAD2) is an about 180-240 amino acids region containing several conserved motifs. Whereas the MAD2 and the REV7 proteins are almost entirely made up of HORMA domains, HOP1 contains a HORMA domain in its N-terminal region and a Zn-finger domain, whose general arrangement of metal-chelating residues is similar to that of the PHD finger, in the C-terminal region. The HORMA domain is found in proteins showing a direct association with chromatin of all crown group eukaryotes. It has been suggested that the HORMA domain recognizes chromatin states that result from DNA adducts, double-stranded breaks or non-attachment to the spindle and acts as an adaptor that recruits other proteins involved in repair [1].

Secondary structure prediction suggests that the HORMA domain is globular and could potentially form a complex β-sheet(s) with associated α-helices [1].

Some proteins known to contain a HORMA domain are listed below:

  • Eukaryotic HOP1, a conserved protein that is involved in meiotic- synaptonemal-complex assembly.
  • Eukaryotic mitotic-arrest-deficient 2 protein (MAD2), a key component of the mitotic-spindle-assembly checkpoint.
  • Eukaryotic REV7, a subunit of the DNA polymerase zeta that is involved in translesion, template-independent DNA synthesis.

We have developed a profile that covers the entire HORMA domain.

Last update:

May 2003 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

HORMA, PS50815; HORMA domain profile  (MATRIX)


Reference

1AuthorsAravind L. Koonin E.V.
TitleThe HORMA domain: a common structural denominator in mitotic checkpoints, chromosome synapsis and DNA repair.
SourceTrends Biochem. Sci. 23:284-286(1998).
PubMed ID9757827



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