The phylogenetic tree reveals that the proteins cluster according to phylogeny of the source organism with S. cerevisiae possesses at least two paralogues, high- and low-affinity K+ transporters.
Folding pattern seen in Trk proteins resembles quadruplicated primitive K+ channels of the VIC superfamily (TC #1.A.1) instead of typical 12 TMS carriers.
[5] This folding pattern resembles quadruplicated primitive K+ channels of the VIC superfamily (TC #1.A.1) instead of typical 12 TMS carriers.
[7] TrkA domains can bind NAD+ and NADH, possibly allowing K+ transporters to be responsive to the redox state of the cell.
The results suggest that KTN is inherently flexible, undergoing a large conformational change through a hinge motion.