Why are We Disagreeing with ID?

If there is such a pathway then what is the problem again? Protein sequences will unavoidably drift apart as nearly neutral or beneficial mutations accumulate in them.

Again, look at the omicron variant spike protein compared to the delta variant:

That’s 32 mutations right there. In the span of about a years worth of viral evolution.

Divergence is typical of all proteins. Literally without a single known exception. There is no known protein family that has remained 100% conserved since it’s inferred origin unless it’s known from only one, or two species that share very recent ancestry. Once geological timescales get involved we see them having diverged from their common ancestors. They’re still doing it now for proteins inferred to have been present in the last universal common ancestor over 3.5 billion years ago.

Abstract

The need to maintain the structural and functional integrity of an evolving protein severely restricts the repertoire of acceptable amino-acid substitutions. However, it is not known whether these restrictions impose a global limit on how far homologous protein sequences can diverge from each other. Here we explore the limits of protein evolution using sequence divergence data. We formulate a computational approach to study the rate of divergence of distant protein sequences and measure this rate for ancient proteins, those that were present in the last universal common ancestor. We show that ancient proteins are still diverging from each other, indicating an ongoing expansion of the protein sequence universe. The slow rate of this divergence is imposed by the sparseness of functional protein sequences in sequence space and the ruggedness of the protein fitness landscape: approximately 98 per cent of sites cannot accept an amino-acid substitution at any given moment but a vast majority of all sites may eventually be permitted to evolve when other, compensatory, changes occur. Thus, approximately 3.5 x 10(9) yr has not been enough to reach the limit of divergent evolution of proteins, and for most proteins the limit of sequence similarity imposed by common function may not exceed that of random sequences.

In so far as they do not function as stators in other protein protein complexes, they’d need to have other functions besides that in order to be useful there. Yes. Obviously. That’s exactly what enables the possibility of evolving larger structures with irreducibly complex functions because the partial/simpler structures can have other functions than the larger one.

No, the other papers that show other functions for parts of the flagella structure particularly for endosymbionts where they function as protein transport systems. Do you even read the papers that get cited? Does evidence matter to you? It should be a concern to you that you’re constantly leaving the impression that it doesn’t.

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