PROSITE documentation PDOC00476Hemerythrin family signature
Marine invertebrates such as annelids or sipunculans possess two completely different types of oxygen binding proteins: globins which are found in the blood and hemerythrins which are found in the vascular system and the coelemic fluid or in muscles (myohemerythrins). Hemerythrins and myohemerythrins [1,2] are small proteins of about 110 to 129 amino acid residues that bind two iron atoms. Five histidines, one glutamic acid and one aspartic acid are involved in the binding of the iron atoms.
Ovohemerythrin [3], a yolk protein from the leech Theromyzon tessulatum seems to belong to this family of proteins, it may play a role in the detoxification of free iron after a blood meal.
A number of uncharacterized bacterial and archaeal proteins are evolutionary related to hemerythrins.
As a signature pattern we selected a region, located in the central section of these proteins and that contains four of the iron-ligands: three histidines and a glutamate or glutamine.
Last update:May 2004 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Sheriff S. Hendrickson W.A. Smith J.L. |
Title | Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution. | |
Source | J. Mol. Biol. 197:273-296(1987). | |
PubMed ID | 3681996 |
2 | Authors | Uchida T. Yano H. Satake K. Kubota I. Tsugita A. |
Title | The amino acid sequence of hemerythrin from Siphonosoma cumanense. | |
Source | Protein Seq. Data Anal. 3:141-147(1990). | |
PubMed ID | 2362933 |
3 | Authors | Baert J.-L. Britel M. Sautiere P. Malecha J. |
Title | Ovohemerythrin, a major 14-kDa yolk protein distinct from vitellogenin in leech. | |
Source | Eur. J. Biochem. 209:563-569(1992). | |
PubMed ID | 1425663 |
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