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. Author manuscript; available in PMC: 2014 Jun 17.
Published in final edited form as: Curr Opin Cell Biol. 2013 Mar 13;25(3):289–296. doi: 10.1016/j.ceb.2013.02.017

Figure 1.

Figure 1

Schematic diagrams of the Tet proteins. Three conserved domains are indicated in mouse Tet proteins, including CXXC zinc finger, cysteine-rich region (Cys-rich), and the double-stranded β-helix (DSBH) fold of the 2OG-dependent and Fe(II)-dependent dioxygenase domain (2OGFeDO). Note that Tet3 has a shorter form, which starts at amino acid 136, that does not contain the CXXC domain. For the 2OGFeDO domain, a multiple sequence alignment of selected JBP/Tet family proteins is shown. Sequences used in the alignment include the Trypanosoma brucei JBP1 (Q9U6M3) and JBP2 (Q57X81); human TET1 (NP_085128), TET2 (NP_001120680), and TET3 (ADU77107); and mouse Tet1 (NP_001240786), Tet2 (ACY38292), and Tet3 (ADR57137). Predicted Fe(II) and 2OG-binding sites are indicated, and the conserved strands that constitute the DSBH fold are shown above the multiple sequence alignment. Numbers represent the amino acid numbers.