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We report the finding of an Agaricus specimen in the section Sanguinolenti and describe it as a new species Agaricus hortusdamarum. Based on ITS data, the species is distinct and well separated from all known sequenced species within this section. The type specimen grew in late autumn, under Cupressus sempervirens, near a Pinus pinea alley in the Villa Borghese Gardens in Rome, in Italy. The new species is phylogenetically close to Agaricus iranicus, a rare species of temperate climate, which is so far described only in the Guilan province in Iran. Its morphological characters and phylogenetic pattern are described and divergence from A. iranicus is discussed.

We report the finding of an Agaricus specimen in the section Sanguinolenti and describe it as a new species Agaricus hortusdamarum. Based on ITS data, the species is distinct and well separated from all known sequenced species within this section. The type specimen grew in late autumn, under Cupressus sempervirens, near a Pinus pinea alley in the Villa Borghese Gardens in Rome, in Italy. The new species is phylogenetically close to Agaricus iranicus, a rare species of temperate climate, which is so far described only in the Guilan province in Iran. Its morphological characters and phylogenetic pattern are described and divergence from A. iranicus is discussed.

Cysteines are among the rarest amino acids in nature, and are both functionally and structurally very important for proteins. The ability of cysteines to form disulfide bonds is especially relevant, both for constraining the folded state of the protein and for performing enzymatic duties. But how does the variation record of human proteins reflect their functional importance and structural role, especially with regard to deleterious mutations? We created HUMCYS, a manually curated dataset of single amino acid variants that (1) have a known disease/neutral phenotypic outcome and (2) cause the loss of a cysteine, in order to investigate how mutated cysteines relate to structural aspects such as surface accessibility and cysteine oxidation state. We also have developed a sequence-based in silico cysteine oxidation predictor to overcome the scarcity of experimentally derived oxidation annotations, and applied it to extend our analysis to classes of proteins for which the experimental determination of their structure is technically challenging, such as transmembrane proteins. Our investigation shows that we can gain insights into the reason behind the outcome of cysteine losses in otherwise uncharacterized proteins, and we discuss the possible molecular mechanisms leading to deleterious phenotypes, such as the involvement of the mutated cysteine in a structurally or enzymatically relevant disulfide bond., SCOPUS: ar.j, FLWIN, info:eu-repo/semantics/published