{PDOC00083} {PS00088; SOD_MN} {BEGIN} ****************************************************** * Manganese and iron superoxide dismutases signature * ****************************************************** Manganese superoxide dismutase (EC 1.15.1.1) (SODM) [1] is one of the three forms of an enzyme that catalyzes the dismutation of superoxide radicals. The four ligands of the manganese atom are conserved in all the known SODM sequences. These metal ligands are also conserved in the related iron form of superoxide dismutases [2,3]. We selected, as a signature, a short conserved region which includes two of the four ligands: an aspartate and a histidine. -Consensus pattern: D-x-[WF]-E-H-[STA]-[FY](2) [D and H are manganese/iron ligands] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2004 / Pattern and text revised. [ 1] Bannister J.V., Bannister W.H., Rotilio G. "Aspects of the structure, function, and applications of superoxide dismutase." CRC Crit. Rev. Biochem. 22:111-180(1987). PubMed=3315461 [ 2] Parker M.W., Blake C.C.F. "Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures." FEBS Lett. 229:377-382(1988). PubMed=3345848 [ 3] Smith M.W., Doolittle R.F. "A comparison of evolutionary rates of the two major kinds of superoxide dismutase." J. Mol. Evol. 34:175-184(1992). PubMed=1556751 -------------------------------------------------------------------------------- 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}