{PDOC51401}
{PS51401; CHORD}
{BEGIN}
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* CHORD domain profile *
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Cysteine- and  histidine-rich  domains (CHORDs) are 60-amino acid modules that
bind two  zinc  ions. They are usually arranged in tandem and are found in all
tested eukaryotes,  with  the  exception  of yeast, where they are involved in
processes ranging  from  pressure  sensing  in  the  heart  to  maintenance of
diploidy in   fungi,   and   exhibit   distinct   protein-protein  interaction
specificity. Six  cysteine and two histidine residues are invariant within the
CHORD domain.  Three  other residues are also invariant and some positions are
confined to positive, negative, or aromatic amino acids [1,2].

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

 - Plant  protein  Required for Mla12 Resistance (RAR1), a common component in
   the signaling pathways triggered by many resistance (R) proteins.
 - Caenorhabditis  elegans  CHORD  containing  protein (chp). It plays a vital
   role in germline development and embryogenesis.
 - Vertebrate  cysteine  and histidine-rich domain-containing protein 1 (CHORD
   domain-containing protein  1),  a  target for transcriptional activation by
   heat-shock factor 1 (HSF1).
 - Mammalian  integrin  beta-1-binding protein 2 (melusin). It may play a role
   during maturation and/or organization of muscles cells.

The profile we developed covers the entire CHORD domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: August 2008 / First entry.

[ 1] Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C.,
     Schulze-Lefert P.
     "A novel class of eukaryotic zinc-binding proteins is required for
     disease resistance signaling in barley and development in C.
     elegans."
     Cell 99:355-366(1999).
     PubMed=10571178
[ 2] Heise C.T., Le Duff C.S., Boter M., Casais C., Airey J.E., Leech A.P.,
     Amigues B., Guerois R., Moore G.R., Shirasu K., Kleanthous C.
     "Biochemical characterization of RAR1 cysteine- and histidine-rich
     domains (CHORDs): a novel class of zinc-dependent protein-protein
     interaction modules."
     Biochemistry 46:1612-1623(2007).
     PubMed=17279625; DOI=10.1021/bi062174k

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