LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| Description | The DOMON domain is an 110-125 residue long domain which has been identified in the physiologically important enzyme dopamine beta-monooxygenase and inseveral other secreted and transmembrane proteins from both plants and animals. It has been named after DOpamine beta-MOnooxygenase N-terminaldomain. The DOMON domain can be found in one to four copies and in association with other domains, such as the Cu-ascorbate dependent monooxygenase domain,the epidermal growth factor domain, the trypsin inhibitor-like domain (TIL), the SEA domain and the Reelin domain [ ]. The DOMON domain may be involved in heme and sugar recognition [].The sequence conservation is predominantly centred around patches ofhydrophobic residues. The secondary structure prediction of the DOMON domain points to an all-β-strand fold with seven or eight core strands supportedby a buried core of conserved hydrophobic residues. There is a chraracteristic motif with two small positions (Gly or Ser) corresponding to a conserved turnimmediately C-terminal to strand three. It has been proposed that the DOMON domain might form a β-sandwich structure, with the strands distributed intotwo beta sheets as is seen in many extracellular adhesion domains such as the immunoglobulin, fibronectin type III, cadherin and PKD domains []. |
| Short Name | DOMON_domain |
