| Type: | Family | Name: | Uncharacterised protein family YjbK |
| Description: | Detailed sequence analysis shows that members of this family are distantly related to thermophilic adenylate cyclases (class 2) () and mammalian thiamine triphosphatases, and belong to the CYTH domain superfamily []. It has been predicted that CYTH domain proteins may play a central role in the interface between nucleotide and polyphosphate metabolism []. Based on the conservation of catalytic residues, it has been predicted that CYTH domains are likely to chelate two divalent cations, and exhibit a reaction mechanism that is dependent on two metal ions, analogous to nucleotide cyclases, polymerases and certain phosphoesterases []. It has also been suggested that the experimentally characterised members of the CYTH domain superfamily, namely adenylyl cyclase and thiamine triphosphatase, are secondary derivatives of proteins that performed an ancient role in polyphosphate and nucleotide metabolism []. | Short Name: | Uncharacterised_YjbK |
