{PDOC51549} {PS51549; DM13} {BEGIN} *********************** * DM13 domain profile * *********************** The DM13 domain has been identified in animal proteins containing a DOMON domain (see ) likely to function as cytochromes involved in as yet unidentified redox reactions potentially related to protein hydroxylation or oxidative cross-linking. However, it is also found in bacteria. The DM13 domain contains a nearly absolutely conserved cysteine, which can be potentially involved in a redox reaction either as a nacked thiol group or by binding a prosthetic group like heme [1]. The DM13 domain is predicted to have a beta-strand-rich fold [1]. The profile we developed covers the entire DM13 domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: October 2011 / First entry. [ 1] Iyer L.M., Anantharaman V., Aravind L. "The DOMON domains are involved in heme and sugar recognition." Bioinformatics 23:2660-2664(2007). PubMed=17878204; DOI=10.1093/bioinformatics/btm411 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}