Table 4.
Potentially novel functional sites
cluster ID | Size | FC | Putative annotation | Distinguishing features |
---|---|---|---|---|
Clust4-Sub23 | 5* | 8.79 | Structural role | Extended beta sheet environment with repeated CYS flanked by PHE. * Several sites are adjacent to one another, and may be involved in disulfide bonds. |
Clust5-Sub70 | 12 | 3.07 | TYR phosphorylation site, possibly autocatalytic | 2/3 of proteins are TYR kinases with multiple phosphorylation sites. Environment characterized by loop containing CYS, MET, and TYR. |
Clust6-Sub240 | 5 | 4.33 | Associated with ligand binding | 80% of sites are near a bound ligand. |
Clust8-Sub25 | 11 | 4.12 | Structural role | Inward facing CYS on a surface accessible helix surrounded by an abundance of aliphatic, hydrophobic sidechains. |
Clust8-Sub352 | 6 | 4.18 | Structural role | Helical CYS in the vicinity of 1 HIS and several aliphatic, hydrophobic sidechains. |
Clust15-Sub152 | 6 | 4.43 | Associated with enzymatic activity | All proteins are enzymes. Environment contains multiple ARG and occasionally HIS. |
Clust21-Sub48 | 9* | 3.06 | Associated with WD repeat motif | Environment characterized by beta sheets and the presence of another CYS. * Several sites are adjacent to one another. |
Clust24-Sub17 | 5 | 4.34 | Functional role | Environment contains an ASP, a GLU, and usually at least one LYS, all charged and polar residues. |
Clust25-Sub19 | 5 | 6.32 | Associated with sugar kinases | Beta sheet environment with multiple sulfur- containing residues. |
Clust31-Sub18 | 5 | 7.00 | Protein binding | 80% of proteins are protein-binding. Environment characterized by helical CYS and an opposing TRP residue. |
Clust36-Sub127 | 5 | 5.04 | Functional role | Environment is solvent exposed with an ASP and LYS forming a possible triad with the CYS. |
Clust39-Sub58 | 5 | 18.34 | Associated with viral proteins | Sparse environment containing TRP, TYR, THR, and ARG, all polar and mostly hydrophobic residues. |
These predictions represent clusters where the function is not obvious but reasonable evidence exists for a coherent functional theme, even if it is in a structural role. FC = functional coherence.