 Protein motif

A protein motif is a recognizable recurring pattern in a protein's sequence or three-dimensional arrangement. A protein sequence motif describes characteristic residues and allowed variation; a protein structural motif describes a recurring spatial combination of structural elements. A motif can be part of a protein domain, without by itself being an independently folding domain or specifying the whole protein's function.

Sequence-pattern notation makes a useful distinction explicit. PROSITE uses defined residues, alternatives and wildcard positions to describe signatures found in protein sequences.^[ref] For an original illustration, take the invented four-position pattern A-x-G-x, with each x allowed any of 20 standard amino acids. It matches $20^2=400$ different residue strings. Finding a match therefore does not uniquely identify a sequence, much less prove a particular biochemical activity. This teaching pattern is not asserted to be a real biological signature.

The EF hand supplies a structural example: two alpha helices flank a loop associated with calcium ion binding in canonical members. Recognizing the arrangement, measuring binding and determining its physiological role are different kinds of evidence.^[ref]

Motifs are useful because local arrangements can recur in proteins with different overall architectures. A sequence signature can guide comparison or experimentation; a structure can test whether the relevant residues approach one another in space. Neither the word “motif” nor a pattern hit alone supplies an affinity measurement or a complete functional annotation.