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- * Cytidine and deoxycytidylate deaminases zinc-binding region signature *
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-
- Cytidine deaminase (EC 3.5.4.5) (cytidine aminohydrolase) catalyzes the
- hydrolysis of cytidine into uridine and ammonia while deoxycytidylate
- deaminase (EC 3.5.4.12) (dCMP deaminase) hydrolyzes dCMP into dUMP. Both
- enzymes are known to bind zinc and to require it for their catalytic activity
- [1,2]. These two enzymes do not share any sequence similarity with the
- exception of a region that contains three conserved histidine and cysteine
- residues which are thought to be involved in the binding of the catalytic zinc
- ion.
-
- Such a region is also found in two other proteins that are highly similar [3]
- to deoxycytidylate deaminase; these proteins are:
-
- - A 21 Kd protein in the comE operon from Bacillus subtilis. This operon is
- required for the binding and uptake of transforming DNA.
- - Caenorhabditis elegans hypothetical protein ZK643.2.
-
- We have derived a signature pattern for this zinc-binding region.
-
- -Consensus pattern: [CH]-A-E-x-[STN]-A-[LIVM]-x(18,26)-P-C-x(2)-C-x(3)-[LIVM]-
- x-[EQ]
- [The C's and H are zinc ligands]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
- -Last update: June 1994 / Pattern and text revised.
-
- [ 1] Yang C., Carlow D., Wolfenden R., Short S.A.
- Biochemistry 31:4168-4174(1992).
- [ 2] Moore J.T., Silversmith R.E., Maley G.F., Maley F.
- J. Biol. Chem. 268:2288-2291(1993).
- [ 3] Bairoch A.
- Unpublished observations (1993).
-