Protein common binding motif

Iron-sulfur proteins are a group of enzymes and other electron carriers that contain clusters of iron and sulfide linked directly to amino-acyl side chains, usually cysteines. They are widely distributed in nature. Soon after their discovery. Hall et al. (1971) proposed that they could be used to follow the course of evolution. Studies of genome sequences have revealed that iron-sulfur cluster binding motifs are among the most commonly recognized sequences. 

The AdoMet binding motif is similar to the Rossmann fold, which is well known from the nucleotide binding proteins [22]. It has been shown that the known crystal structures of methyltransferases are strikingly similar in the AdoMet-binding regions [23], which indicates that all AdoMet-utilizing enzymes may share a common divergent evolution. 

Regulatory proteins are DNA-binding proteins that recognize specific DNA sequences most have distinct DNA-binding domains. Within these domains, common structural motifs that bind DNA are the helix-turn-helix, zinc finger, and homeodomain. 

Another DNA-binding motif very common in eukaryotic regulatory proteins is the zinc finger. This motif was first identified as the DNA-binding structure in the RNA poly-... 

Vallely et al., 2002 Ikura and Ames, 2006). The C-terminal EF-hand contains the classical Ca2+-binding motif, common to all EF-hand proteins (see above). This Ca2+-binding motif has a typical sequence signature of 12 amino acids and is flanked by helices Hin and HIV. The N-terminal EF-hand is different from the classical EF-hand motif and is characteristic of the S100 proteins. Therefore, this EF-hand, with a 14 amino acid consensus sequence motif, is flanked by helices H, and Hn and is called the SlOO-specific or pseudo EF-hand. 

The evolution of protein structures shows conservation in recognition features for common binding sites. For example, the adenosine triphosphate (ATP)/ guanosine triphosphate (GTP) binding site contains an amino acid motif A (P-... 

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