Name
Abstract | ||
|---|---|---|
Tiki proteins appear to antagonize Wnt signalling pathway by acting as Wnt proteases, thereby affecting Wnt solubility by its amino-terminal cleavage. Tiki1 protease activity was shown to be metal ion-dependent and was inhibited by chelating agents and thus was tentatively proposed to be a metalloprotease. Nevertheless, Tiki proteins exhibit no detectable sequence similarity to previously described metalloproteases, but instead have been reported as being homologues of TraB proteins (Pfam ID: PF01963), a widely distributed family of unknown function and structure. Here, we show that Tiki proteins are members of a new superfamily of domains contained not just in TraB proteins, but also in erythromycin esterase (Pfam ID: PF05139), DUF399 (domain of unknown function 399; Pfam ID: PF04187) and MARTX toxins that contribute to host invasion and pathogenesis by bacteria. We establish the core fold of this enzymatic domain and its catalytic residues. |
Year | DOI | Venue |
|---|---|---|
2013 | 10.1093/bioinformatics/btt412 | BIOINFORMATICS |
Field | DocType | Volume |
Sequence alignment,Wnt signaling pathway,Proteases,Metalloproteinase,Biology,Biochemistry,Domain of unknown function,Hedgehog signaling pathway,Protease,Bioinformatics,Peptide sequence | Journal | 29 |
Issue | ISSN | Citations |
19 | 1367-4803 | 0 |
PageRank | References | Authors |
0.34 | 4 | 2 |
Name | Order | Citations | PageRank |
|---|---|---|---|
| Luis Sánchez-Pulido | 1 | 2 | 3.16 |
| Chris P. Ponting | 2 | 733 | 283.28 |