The SignalP 5.0 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 5.0 can discriminate between three 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). SignalP 5.0 is based on a deep convolutional and recurrent neural network architecture including a conditional random field.