| Ydc2 protein domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystal structure of the yeast mitochondrial Holliday junction resolvase, YDC2 | |||||||||
| Identifiers | |||||||||
| Symbol | Ydc2-catalyst | ||||||||
| Pfam | PF09159 | ||||||||
| Pfam clan | CL0219 | ||||||||
| InterPro | IPR015242 | ||||||||
| SCOP2 | 1kcf / SCOPe / SUPFAM | ||||||||
| CDD | cd00529 | ||||||||
| |||||||||
In molecular biology, the protein domain, Ydc2 (also known as SpCce1), is a Holliday junction resolvase from the fission yeast Schizosaccharomyces pombe that is involved in the maintenance of mitochondrial DNA.
The Ydc2 domains are enzymes (or "biological catalysts") that resolve Holliday junctions into separate DNA duplexes by cleaving DNA after 5'-CT-3, and 5'-TT-3, sequences.
The junction resolving enzymes are very diverse, but have the following properties in common:
Essentially, they are highly specific.
Furthermore, the cleavage efficiency is affected by:
This protein domain forms a ribonuclease H fold consisting of two beta sheets and one alpha helix, arranged as a beta-alpha-beta motif. Each beta sheet has five strands, arranged in a 32145 order, with the second strand being antiparallel to the rest. [2]