ultimum. The secretome of P. ultimum was identi fied by predicting secreted proteins using the PexFinder algorithm in conjunction with the TribeMCL pro tein family clustering algorithm. The P. ultimum secre selleck chemicals tome is composed of 747 proteins that can be clustered into 195 families Inhibitors,Modulators,Libraries and 127 singletons. Of these, two families and one singleton encode transposable element related proteins that were missed in the repeat masking process. The largest family contains 77 members, mostly Inhibitors,Modulators,Libraries ankyrin repeat containing proteins, of which only 3 were predicted to have a signal peptide. Notable families of secreted proteins include protease inhibitors, NPP1 like proteins, cellulose binding elicitor lectin like proteins with carbohydrate binding domains, elicitins and elicitin like proteins, secreted E3 ubiquitin Inhibitors,Modulators,Libraries ligases, cell wall degrading enzymes, lipases, phospholipases, poten tial adhesion proteins, highly expanded families of pro teases and cytochrome P450, and several families of unknown function.

A subset of the secretome showed exclusive similarity to fungal sequences yet are absent in other eukaryotes. These may represent shared pathogenicity proteins for filamentous plant pathogens, such as perox idases, CBEL Inhibitors,Modulators,Libraries like proteins, and various cell wall degrading enzymes and other hydrolases. RXLR Inhibitors,Modulators,Libraries effectors Many plant pathogens, especially biotrophic and hemi biotrophic ones, produce effector proteins that either enter into host cells or are predicted to do so. The genomes of Ph. sojae, Ph. ramorum and Ph.

infes tans encode large numbers of potential effector proteins that contain an amino terminal cell entry domain with the motifs RXLR and dEER, which mediate entry of these proteins into host cells in the absence of pathogen encoded machinery. RXLR dEER effectors are thought, and in a few cases shown, to suppress host defense responses, but a subset of these selleck effectors can be recognized by plant immune receptors resulting in programmed cell death and dis ease resistance. To search for RXLR effectors in the gen ome of P. ultimum, we translated all six frames of the genome sequence to identify all possible small proteins, exclusive of splicing. Among these, a total of 7,128 translations were found to contain an amino terminal signal peptide based on SignalP prediction. We then used the RXLR dEER Hidden Markov Model to search the translations for candidate effectors and, as a control, the same set of translations following permutation of their sequences downstream of the sig nal peptide. Only 35 sequences with signifi cant scores were found in the non permuted set while an average of 5 were found in 100 different permuted sets. In comparison to the Ph. ramorum secretome, 300 hits were found without permutation.