I think what CrystalDragon was alluding to is the fact it's possible to have a similar experience and arrive at an entirely different world-view or belief.
I know for myself I went on a 'spiritual quest' of sorts back when I thought I needed religion in my life. But after seeking out and learning about all sorts of spiritual/religious beliefs, ultimately I arrived at a state of non-belief. And the effect was incredible; like there had been this giant weight on my shoulders and suddenly it was gone and everything seemed so clear. It was a rush of emotion and incredible relief, and all it took was acknowledging and coming to terms with what I honestly believed deep down.
Quite the experience.
Just to clarify though, I found non-belief. Ultimately I adopted an agnostic position; I believe that if there is some sort of supernatural deity in the universe it is likely unknown to us and not represented in any particular theistic beliefs. But that's just my view of things.
Good grief man, you're like a broken record.
Summary of the evolutionary model for the origin of the flagellum, showing the six major stages and key intermediates. White components have identified or reasonably probable nonflagellar homologs; grey components have either suggested but unsupported homologs, or no specific identified homologs, although ancestral functions can be postulated. The model begins with a passive, somewhat general inner membrane pore (1a) that is converted to a more substrate-specific pore (1b) by binding of proto-FlhA and/or FlhB to FliF. Interaction of an F1F0-ATP synthetase with FlhA/B produces an active transporter, a primitive type III export apparatus (1c). Addition of a secretin which associates with the cytoplasmic ring converts this to a type III secretion system (2). A mutated secretion substrate becomes a secreted adhesin (or alternatively an adhesin is coopted by transposition of the secretion recognition sequence), and a later mutation lets it bind to the outer side of the secretin (3a). Oligomerization of the adhesin produces a pentameric ring, allowing more surface adhesins without blocking other secretion substrates (3b). Polymerization of this ring produces a tube, a primitive type III pilus (4a; in the diagram, a white axial structure is substituted for the individual pilin subunits; all further axial proteins are descended from this common pilin ancestor). Oligomerization of a pilin produces the cap, increasing assembly speed and efficiency (4b). A duplicate pilin that loses its outer domains becomes the proto-rod protein, extending down through the secretin and strengthening pilus attachment by association with the base (4c). Further duplications of the proto-rod, filament, and cap proteins, occurring before and after the origin of the flagellum (6) produce the rest of the axial proteins; these repeated subfunctionalization events are not shown here. The protoflagellum (5a) is produced by cooption of TolQR homologs from a Tol-Pal-like system; perhaps a portion of a TolA homolog bound to FliF to produce proto-FliG. In order to improve rotation, the secretin loses its binding sites to the axial filament, becoming the proto-P-ring, and the role of outer membrane pore is taken over by the secretin’s lipoprotein chaperone ring, which becomes the proto-L-ring (5b). Perfection of the L-ring and addition of the rod cap FlgJ muramidase domain (which removes the necessity of finding a natural gap in the cell wall) results in 5c. Finally, binding of a mutant proto-FliN (probably a CheC receptor) to FliG couples the signal transduction system to the protoflagellum, producing a chemotactic flagellum (6); fusion of proto-FliN and CheC produces FliM. Each stage would obviously be followed by gradual coevolutionary optimization of component interactions. The origin of the flagellum is thus reduced to a series of mutationally plausible steps.
Evolution of the bacterial flagellum
Last year, Pallen and Matzke (2006) presented a discussion of how bacterial flagella may have evolved, based in large part on comparisons of sequences from the various protein components. Many of the proteins that make up a flagellum have homologues that serve non-flagellar functions, strongly suggesting that they were co-opted from pre-existing proteins during the evolution of flagella. (See Matzke’s detailed model of flagellar evolution here and a video based on it here, and Ken Miller talking about flagella here). Specifically, there is ever-mounting evidence that bacterial flagella and the type III secretory system (TTSS) that toxic bacteria use to inject their prey are descended from the same ancestral structure. The fact that the TTSS lacks many of the proteins in flagella but remains functional (for toxin injection rather than locomotion) clearly indicates that not all the parts need to be present for some function to be carried out by the structure.
Genome sequences reduce the complexity of bacterial flagella. « Genomicron
