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. 2019 Nov 25;10:1449. doi: 10.3389/fpls.2019.01449

Figure 1.

Figure 1

Mitochondrial iron transporters in Arabidopsis exhibit sequence conservation for the residues significant for mitochondrial Fe transport. Sequence alignment of Arabidopsis AtMIT1 and AtMIT2 with mitoferrins from rice (OsMIT), yeast (ScMRS3, ScMRS4) and human (HsMfrn1) generated using CLUSTAL O. Sequences of the six predicted transmembrane helices on these proteins are depicted by H1-H6. The Mitochondrial Energy Transfer Signature (METS-P-x-[DE]-x-[LIVAT]-[RK]-x-[LRH]-[LIVMFY]-[QGAIVM]) identified in AtMIT1 and AtMIT2 is indicated by the purple boxes. The putative Fe-binding motifs are underlined in green, and the residues implicated in Fe transport are indicated in red boxes (MIT1 Fe binding motifs: H53, H110, M196, Y235). Conserved [DE]-xx-[RK] motifs putatively forming the salt bridges on the cytosolic and the matrix side of the membrane are indicated in yellow and blue boxes, respectively. An * (asterisk) indicates positions which have a single, fully conserved residue. A : (colon) indicates conservation between groups of strongly similar properties (roughly equivalent to scoring > 0.5 in the Gonnet PAM 250 matrix). A . (period) indicates conservation between groups of weakly similar properties (roughly equivalent to scoring =< 0.5 and > 0 in the Gonnet PAM 250 matrix).