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Additional file 2: Fig. S1. Average Nucleotide Identity (ANI) matrix between all 132 compared picocyanobacteria from SCs 5.1, 5.2 and 5.3.

Additional file 18: Fig. S4. Phylogenetic analysis of picocyanobacterial Ni/Cu/Zn/Fe/Mn superoxide dismutases. The Ni-type maturation protease from marine strains was used to root the tree. Bootstrap values >75 are shown and the habitat of each picocyanobacterial enzyme is color coded.

Additional file 4: Fig. S2. A) Cross-comparison of strict core, soft core, shell and cloud in all 132 picocyanobacteria from all habitats and SCs. B) Plots estimating the core genome (n° of genes) and pangenome (n° of genes) of all three SCs. C) Functionality of the meta-pangenome of picocyanobacteria assessed by SEED/KEGG. Each gene category is color coded for the shared (strict core, soft core) and flexible (shell and cloud) genome.

Additional file 20: Fig. S5. Total number (Y axis) of A) transposases and B) integrases found in freshwater, brackish and marine picocyanobacteria.

Additional file 12: Fig. S3. Genomic context of the phoBR two-component system in different marine, brackish and freshwater cluster 5 picocyanobacteria. Each subunit is color coded accordingly. The right panel shows a phylogenomic tree with all those freshwater strains (colored red) possessing two copies of the phoB gene.

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Additional file 5: Fig. S5A-B. Uncropped SDS-PAGE gels and Western blot images included in the manuscript.

Additional file 1: Fig. S1. Inhibition profile of FhCL3 propeptide against recombinant parasite and human cysteine and serine peptidases.

Additional file 6: Fig. S6A-B. Antibodies against FhCL3 zymogen differentially recognize the recombinant FhCL3 zymogen, mature domain and propeptide segment.

Additional file 2: Fig. S2. Recombinant expression of the variant FhCL3 propeptides.

Additional file 4: Fig. S4. Alignment of the F. hepatica and human cathepsin peptidases.

Additional file 3: Fig. S3A-E. Inhibition constant of the FhCL3 propeptide and its variants against F. hepatica and human cathepsin peptidases.

Congenital heart disease (CHD) patients have an increased prevalence of extracardiac congenital anomalies (CAs) and risk of neurodevelopmental disabilities (NDDs). Exome sequencing of 1213 CHD parent-offspring trios identified an excess of protein-damaging de novo mutations, especially in genes highly expressed in the developing heart and brain. These mutations accounted for 20% of patients with CHD, NDD, and CA but only 2% of patients with isolated CHD. Mutations altered genes involved in morphogenesis, chromatin modification, and transcriptional regulation, including multiple mutations in RBFOX2, a regulator of mRNA splicing. Genes mutated in other cohorts examined for NDD were enriched in CHD cases, particularly those with coexisting NDD. These findings reveal shared genetic contributions to CHD, NDD, and CA and provide opportunities for improved prognostic assessment and early therapeutic intervention in CHD patients.

The superimposition of the FFA1 crystal structure and a characteristic conformation of FFA1 from conformational search of the FFA1 crystal structure without the ligand. (PDF 309Â kb)

The hydrogen bonding network involving water molecules in FFA1. (PDF 269Â kb)

Sequence alignment of the free fatty acid receptors. (PDF 235Â kb)

Superimposition of 25 FFA2 homology models built based on 25 GPCRs with an available crystal structure. (PDF 246Â kb)

The binding cavities in the FFA1 crystal structure (A), rhodopsin (B) and β2 adrenergic receptor (C) based FFA1 homology models. (PDF 416 kb)

Agonist binding at the FFA1 crystal structure. (PDF 415Â kb)

Sequence identity (%) in the transmembrane helices of the FFA receptors and 25 GPCRs with available crystal structures. (PDF 343Â kb)

The location of putative allosteric sites at FFA1-3. (PDF 310Â kb)

Sequence alignment of the free fatty acid receptors and 25 GPCRs with available crystal structures and HHpred server predictions of a homologous relationship. (PDF 329Â kb)