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Example sentences for: ec-

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Ec-MoeB, Mt-MoeBR, Pa-MoeB, Pa-MoeBR, and Sc-MoeBR all contain two pairs of cysteine residues, each arranged in a CXXC motif and spaced 68-70 residues apart, like those in ThiF proteins (arrows in Figures 2cand 3).
All 12 sequences in this region have high similarity to the derived consensus sequence GXGXXG(7X)A(SX)GXGXXG(4X)D(9X)R, which defines a nucleotide binding motif [ 16 25 ] . In addition, all sequences have five residues, or conservative substitutions in the case of Pa-MoeB, shown to participate in the adenylation reaction catalyzed by Ec-MoeB (Figure 3) [ 7 ] . The fact that such high similarities are retained in the ThiF coding region across three bacterial divisions suggests that this domain functions more or less autonomously.
All of the predicted amino acid sequences except Ec-MoeB, Mlo-MoeZdR, and Pa-MoeB also have C-terminal similarity (BLAST E value < 1 -12) to a rhodanese-like domain (Pfam00581) (Figure 2c, Table 2) [ 26 ] . Rhodanese, a thiosulfate:cyanide sulfurtransferase (EC 2.8.
MoeBR has the ThiF and 2X CXXC domains configured like MoeB but includes an N-terminal rhodanese-like domain, the polyproline motif, and has a Y substitution at position 155 (Ec-MoeB numbering).
MoeB, exemplified by Ec-MoeB, and MoeBR, exemplified by cnxF of Aspergillis nidulans [ 16 ] , participate in the synthesis of MPT-Mo as MSAEs.