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. 2020 Jun 29;12(7):702. doi: 10.3390/v12070702

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Sequence alignments and hallmark features of orthoreovirus FAST proteins and secondary polycistronic genome segment ORFs. (A) Sequence alignments of the p10 FAST proteins encoded by the indicated three orthoreovirus species or proposed species. Residues conserved in all three species are highlighted in cyan while the four conserved cysteines are highlighted in yellow. Hallmark p10 motifs are indicated: Noose, cystine noose formed by Cys9-Cys21; CM, conserved multimerization motif; TM, transmembrane domain; FA, palymitoylated di-cysteine motif; PB, polybasic motif with basic residues in red boldface; AH, predicted amphipathic helix underlined. (B) Sequence alignments of the p17 proteins encoded by the indicated fusogenic orthoreovirus species or proposed species. Lowercase labels denote isolates within a species: ch and tu are chicken and turkey isolates of ARV; bu and ps are bulbul and psittacine isolates of ARVN; Pu is the Pulau isolate of NBV. Residues conserved in all alignments are highlighted in cyan. Residues in p17 that are conserved in at least one isolate from two of the three virus species are shaded green. (C) Sequence alignments of the p16 proteins encoded by the indicated fusogenic orthoreovirus species or proposed species. Residues conserved in all alignments are highlighted in cyan. Residues shaded green are conserved in two of the three virus species (D) Sequence alignments of the p13, p14, and p15 FAST proteins encoded by the indicated five orthoreovirus species or proposed species. Alignments were generated using Clustal Muscle and manually adjusted to align the indicated hallmark structural and functional motifs of FAST proteins: FA, fatty acid myristoylation motif (GXXXS); TM, transmembrane domain; PB, polybasic motif, basic residues in boldface; AH, predicted amphipathic helix (underlined); PP, polyproline motifs include a PPXY motif in p13/p14 and a polyproline helix (PPAPPP) in p15, shaded grey. The N-terminal decapeptide conserved in p13/p14 is in boldface. Residues conserved in three or more sequences are highlighted in cyan.