The SignalP server predicts the presence of signal peptides and the location of their cleavage sites in proteins from Archaea, Gram-positive Bacteria, Gram-negative Bacteria and Eukarya.
In Bacteria and Archaea, SignalP 6.0 can discriminate between five types of signal peptides:
- Sec/SPI: "standard" secretory signal peptides transported by the Sec translocon and cleaved by Signal Peptidase I (Lep)
- Sec/SPII: lipoprotein signal peptides transported by the Sec translocon and cleaved by Signal Peptidase II (Lsp)
- Tat/SPI: Tat signal peptides transported by the Tat translocon and cleaved by Signal Peptidase I (Lep)
- Tat/SPII: Tat lipoprotein signal peptides transported by the Tat translocon and cleaved by Signal Peptidase II (Lsp)
- Sec/SPIII: Pilin and pilin-like signal peptides transported by the Sec translocon and cleaved by Signal Peptidase III (PilD/PibD)
Additionally, SignalP 6.0 predicts the regions of signal peptides. Depending on the type, the positions of n-, h- and c-regions as well as of other distinctive features are predicted.
SignalP 6.0 is based on a transformer protein language model with a conditional random field for structured prediction.
- Results are given as a graph which show probability of each section of a sequence belonging to a signaling peptide
- There is an extensive guide to help the user understand their results
The user only needs to provide a protein sequence and select the report length to use the tool. The results are simple and quickly identify Sec or Tat signals and cleavage sites.