{PDOC00082}
{PS00087; SOD_CU_ZN_1}
{PS00332; SOD_CU_ZN_2}
{BEGIN}
***********************************************
* Copper/Zinc superoxide dismutase signatures *
***********************************************

Copper/Zinc superoxide dismutase (EC 1.15.1.1) (SODC) [1] is  one of the three
forms of an enzyme that catalyzes the dismutation of superoxide radicals. SODC
binds one atom each  of zinc and copper.  Various forms  of  SODC are known: a
cytoplasmic  form in  eukaryotes, an additional chloroplast form in plants, an
extracellular form in some  eukaryotes, and a periplasmic form in prokaryotes.
The metal binding sites are conserved in all the known SODC sequences [2].

We derived two signature  patterns for this family of enzymes:  the  first one
contains two  histidine residues that  bind the copper atom; the second one is
located in the C-terminal section of  SODC  and  contains a  cysteine which is
involved in a disulfide bond.

-Consensus pattern: [GA]-[IMFAT]-H-[LIVF]-H-{S}-x-[GP]-[SDG]-x-[STAGDE]
                    [The 2 H's are copper ligands]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 5.

-Consensus pattern: G-[GNHD]-[SGA]-[GR]-x-R-x-[SGAWRV]-C-x(2)-[IV]
                    [C is involved in a disulfide bond]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: These patterns will not detect proteins related to SODC, but which have
 lost their catalytic activity, such as Vaccinia virus protein A45.

-Last update: April 2006 / Patterns 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] 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}