Protein Family Models

This motif has been identified in a wide range of bacteria at their C-terminus. It has been suggested that this is a protein sorting signal. Based on phylogenetic profiling it has been suggested that the EpsH family of proteins mediate this function [1]. [1]. 16930487. Exopolysaccharide-associated protein sorting in environmental organisms: the PEP-CTERM/EpsH system. Application of a novel phylogenetic profiling heuristic. Haft DH, Paulsen IT, Ward N, Selengut JD;. BMC Biol. 2006;4:29. (from Pfam)

Date:

2024-10-16

This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding. [1]. 15236739. The PA14 domain, a conserved all-beta domain in bacterial toxins, enzymes, adhesins and signaling molecules. Rigden DJ, Mello LV, Galperin MY;. Trends Biochem Sci. 2004;29:335-339. (from Pfam)

Date:

2024-10-16

DUF3494 domain-containing protein similar to type I ice-binding protein

Date:

2017-03-02

This HMM represents a conserved region of about 90 amino acids, shared in at least 4 distinct large putative proteins from the slime mold Dictyostelium discoideum and 10 proteins from the rumen bacterium Fibrobacter succinogenes, and in no other species so far. We propose here the name fibro-slime domain

Date:

2019-09-10

This model describes a 25-residue domain that includes a near-invariant Pro-Glu-Pro (PEP) motif, a thirteen residue strongly hydrophobic sequence likely to span the membrane, and a five-residue strongly basic motif that often contains multiple Arg residues. In nearly every case, this motif is found within nine residues, and usually within five residues, of the extreme C-terminus of the protein. Proteins with this motif typically have Sec translocation signal sequences at the N-terminus. The PEP-CTERM region typically appears many times per genome (sometimes on over 100 proteins), or not at all, and co-occurs always with an exosortase, analogous (but unrelated) to sortase, the transpeptidase that processes LPXTG sorting signals in Gram-positive bacteria. PEP-CTERM proteins frequently are poorly conserved, low complexity, Ser/Thr-rich proteins that show little resemblance to typical enzymes. Those PEP-CTERM proteins likely undergo extensive glycosylation and then constitute much of the proteinaceous matter that is often found in the extracellular polymeric substance (EPS) of environmental bacterial biofilms.

Date:

2023-07-12