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By Gronwall T.H.

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1b), distinct monophyletic clades of domains are typically determined through comparison of often subtle variations in sequence composition. g. streptokinase), the superantigen/toxin domains, the RnfH family, the aromatic compound monooxygenase TmoB subunit family (40), the RNA-binding TGS family (88), the Mut7-C fused family (41), TAPI phage-tail assembly component Ubls, and the sporadically distributed but related assemblage of various prokaryotic Ubl families, many of which are predicted to act as modifiers (41).

2 Structure and Evolution of Ubiquitin and Ubiquitin-Related Domains 23 other face exposed. The chief interacting positions between the sheet and the helical segment, and the pattern of key stabilizing hydrophobic interactions are conserved throughout the fold, supporting its monophyletic origin. The b-GF domains found in IF3 and the second largest subunit (b-subunit orthologs) of the archaeoeukaryotic RNA polymerase more or less correspond to this conserved core (Fig. 1b). Several b-GF domains display simple structural elaborations of this basic four-stranded core, which can be observed in Fig.

It is quite probable that the phage TAPI is processed by the peptidase domains of TAPK, with the JAB probably releasing the Ubl domain by cleaving at the point of the C-terminal-most glycine of the Ub-domain. Though there is no evidence for this Ubl being incorporated into the mature phage tail, it is possible that it plays a role in assembly of the tail. Mut7C-fused clade. A small yet phyletically diverse superfamily of classical bacterial Ubls is fused to the Mut7-C RNAse domain, a member of the PilT N-terminal (PIN) RNAse fold.

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Conformal Mapping of a Family of Real Conics on Another (1920)(en)(4s) by Gronwall T.H.


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