Fast collapse of a linear homopolymer after a spasmodic temperature decrease or deterioration of the solvent quality results in the initiation of folded nonequilibrium globule. The chain line in it is a fractal with the dimension mu less than or equal to 2 at small ranges and 3 at the large ones. This is provided by non-selfintersection of the chain and initiated therefore spatial segregation from each other at all the ranges of the chain regions, globulized each in itself. Further relaxation of the folded globule proceeds very slowly only at the expense of reptation (diffusion crawling) of the chain along itself, and results in the polymer knotting. The model of the folded globule permits explanation from a single viewpoint of a number of globular proteins properties. Predictions are formulated whose checking in a real or computer experiment should reveal the adequacy of our results.