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To infer tertiary-structure conservation in BBS and CCT8L proteins we predicted the secondary structure for each family from alignments of multiple sequences, excluding structure and sequence information from other families.
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We inferred multiple orthologous relationships between ab initio predicted products with database sequences (excluding mouse database orthologs).
We next collected sequences excluding the original sequences used to conduct the queries.
The same case was true for Psocoptera, with only six sequences excluded, and Trombidiformes, with only one sequence excluded.
We constructed a multiple sequence alignment of YidC excluding the unconserved first transmembrane helix (TM1) and the periplasmic P1 domain.
Multiple sequences were aligned using Clustal X [45].
However, the sequence excluded the canonical choice.
Multiple sequence alignment were performed to exclude vector sequences and to identify redundant (not unique) sequences using the program AlignX (Vector NTI Suite V 8.0, InforMax, Invitrogen, Carisbad, CA, USA) with an engine based on the Clustal W algorithm.
Multiple sequencing of peptides was minimized by excluding the selected peptide candidates for 45 s.
For that purpose, we constructed a multiple sequence alignment of E. coli YidC excluding the nonconserved first transmembrane helix (TM1) and the P1 domain and computed direct evolutionary couplings between pairs of YidC residues (Kamisetty et al., 2013).
For phylogenetic tree construction, the seed sequence was the multiple sequence alignment of FBG domains that excluded truncated FBG domains.
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