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DUF1559 domain-containing protein
A large family of paralogous proteins apparently unique to planctomycetes. (from Pfam)
prepilin-type N-terminal cleavage/methylation domain-containing protein
This short motif directs methylation of the conserved phenylalanine residue. It is most often found at the N-terminus of pilins and other proteins involved in secretion, see Pfam:PF00114, Pfam:PF05946, Pfam:PF02501 and Pfam:PF07596. (from Pfam)
H-X9-DG-CTERM domain-containing protein
This model describes a region of about 20 residues found typically about 30 residues away from the C-terminus of large numbers of proteins in the Planctomycetes, Verrucomicrobia, and Lentisphaerae. Members of this family typically have a prepilin-type N-terminal cleavage and methylation site domain (see TIGR02532), a poorly conserved central region modeled by Pfam HMM PF07596 (currently called DUF1559), and this region near the C-terminus. The lineages in which these member proteins are found are notable for compartmentalization of the cytosol maintained by internal membranes. The motif H-X(9)-D-G is nearly invariant. Single genomes may encode over 200 such proteins.
DUF1559 domain-containing protein containing an N-terminal cleavage/methylation motif often found in pilins
This model describes many but not all examples of the N-terminal region of bacterial proteins that resemble type IV pilins at their N-terminus, with a cleavage site G^FxxxE followed by a hydrophobic stretch. The new N-terminal residue, usually Phe, is methylated. Separate domains of the prepilin peptidase appear responsible for cleavage and methylation. Proteins with this N-terminal region include type IV pilins and other components of pilus biogenesis, competence proteins, and type II secretion proteins. Typically several proteins in a single operon have this N-terminal domain. The N-terminal cleavage and methylation site is described by PROSITE motif PS00409 as [KRHEQSTAG]-G-[FYLIVM]-[ST]-[LT]-[LIVP]-E-[LIVMFWSTAG](14).
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