In human cells, two classes of proteins are known to be involved in RNA editing: the ADAR and APOBEC families.
Currently, four classes of proteinases are known as being capable of breaking down nearly all components of the extracellular matrix: serine proteinases, aspartatic proteases, cystein proteinases and matrix metalloproteinases (MMPs) [ 2- 4].
This level of diversity and expression was comparable to SVMPs in viperids such as Protobothrops flavoviridis[ 43] and Crotalus adamanteus[ 27], although Hypsiglena sp. only had class P-III SVMPs, whereas three classes of SVMP are known from viperids [ 46].
To date, four classes of HDAC are known.
Currently, at least four classes of proteinases are known: serine proteinases, aspartatic proteinases, cystein proteinases and matrix metalloproteinases [ 2- 4].
Three classes of RNRs are known, categorized by the cofactor they use to generate a protein radical required for catalysis.
Three classes of enzymes are known: catechol oxidases oxidize the substrate to the corresponding quinone in a two-electron process at a copper active site.
Typically three classes of recoding are known: 1) frameshift recoding; 2) bypass (hopping) recoding; and 3) codon redefinition involving site-specific recognition (usually but not limited to stop codon).
Examples of pumps with specificity towards one class of quinolone are known; for example, the NorA protein of Staphylococcus aureus has been shown to be involved in the specific efflux of hydrophilic quinolones [106].
As the differences between the two classes of simulated data are known, we use these data to investigate how well the proposed method can discriminate the two classes with sequence features, and how well it can reveal the true differences (i.e., the seeds) between the two classes.
In animals, two main classes of GCs are known to exist, a plasma membrane localized receptor (rGC) class that is activated by ligands and a soluble cytoplasmic (sGC) form that is predominately activated by nitric oxide (NO) [2].
