Notwithstanding low sequence identity (60%), GIMFhelix is functionally an isoenzyme of GST A4-4.
The two enzymes show low sequence identity (27.3%) but the same prototypic architecture and domain organization.
In spite of their low sequence identity, they show surprisingly similar three-dimensional folds.
CaAK acquires a protein fold similar to the other known structures of AKs despite the low sequence identity (<30%).
Helix perturbations are also conserved within a family of membrane proteins despite low sequence identity in the perturbed region.
These proteins share similar folds but have low sequence identity, and differ greatly in both size and activity.
However, the low sequence identity of Pmp23 with the G-type lysozyme (10% over 186 residues) prompted us to revisit this analysis.
A comparison with other known structures reveals that ECAI adopts a protein fold most similar to E. coli fucose isomerase (ECFI) despite very low sequence identity 9.7%.
Spo0F and the N-terminal receiver domain of NtrC (NT-NtrC) have similar topologies but low sequence identity, enabling a test of the effects of sequence on folding.
Despite this low sequence identity, possum IL-2 still possessed the characteristic hallmarks of mammalian IL-2, such as a predicted signal peptide and conserved family motifs.
However, only one Edg GPCR (S1PR1) structure has been determined to date, and it has low sequence identity with the non-Edg GPCRs (<20%).
