The domain within your query sequence starts at position 28 and ends at position 226; the E-value for the HORMA domain shown below is 8.3e-61.

EHESLVVVKKLFATCISCITYLRGLFPESSYRDRRLDDLSLKILREDKKCPGSLHIIKWI
QGCFDALEKRYLHMAVLTLYTNPKEPEKVTEIYQFRFKYTKKGTTMDFDSSSTSFESGTD
SEDIKKACSLLIRQLYILMQNLGPLPNDVILTMKLHYYNSVTPHDYQPPGFKEAVNSHFL
LFEGEPVSLRMGSVSSGFH

HORMA

HORMA
PFAM accession number:PF02301
Interpro abstract (IPR003511):

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 recognises 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 [(PUBMED:9757827)].

Secondary structure prediction suggests that the HORMA domain is globular and could potentially form a complex beta-sheet(s) with associated alpha-helices [(PUBMED:9757827)].

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.

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