Slr0006-like proteins: A TsaC/TsaC2/YciO subfamily exclusive to cyanobacteria

[Display omitted] •We identified a new TsaC/TsaC2/YciO subfamily called the Slr0006-like subfamily.•The Slr0006-like proteins are found exclusively in cyanobacteria.•Each TsaC/TsaC2/YciO subfamily has a specific signature motif in cyanobacteria.•The Slr0006-like proteins have the typical TsaC-domain...

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Bibliographic Details
Published in:Molecular phylogenetics and evolution 2017-04, Vol.109, p.1-10
Main Authors: Carvalho, Leonor L., Salminen, Tiina A., Dahlström, Käthe M.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - chemistry
Bacterial Proteins - classification
Bacterial Proteins - genetics
Binding Sites
Conserved Sequence
Evolution, Molecular
Homology modeling
Molecular Dynamics Simulation
Molecular Sequence Annotation
Molecular Sequence Data
Phylogeny
Protein Domains
Protein evolution
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Sll0216
Sll1866
Structural Homology, Protein
Synechocystis - genetics
tRNA modification
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Summary:[Display omitted] •We identified a new TsaC/TsaC2/YciO subfamily called the Slr0006-like subfamily.•The Slr0006-like proteins are found exclusively in cyanobacteria.•Each TsaC/TsaC2/YciO subfamily has a specific signature motif in cyanobacteria.•The Slr0006-like proteins have the typical TsaC-domain fold with a central cleft.•The central cleft might contribute to the unique function of Slr0006-like proteins. The universally conserved TsaC/TsaC2/YciO family of proteins is essential for the N6-threonylcarbamoyladenosine modification present in almost all ANN-decoding tRNAs. Previously, the family has been grouped into the TsaC/TsaC2 and YciO subfamilies. We used sequence analysis, phylogenetic methods and homology modeling to show that a third subfamily, the Slr0006-like subfamily, exists exclusively in some cyanobacteria. The Slr0006-like proteins are solely found together with both TsaC and YciO homologs, indicating a distinct function for the Slr0006-like subfamily. Accordingly, the homology models show that the amino acids in their putative binding clefts differ significantly. Hence, we introduce a new cyanobacterial subfamily of proteins with the TsaC-domain fold, along with the generated classification rules to assign new members to the correct cyanobacterial subfamily.
ISSN:1055-7903
1095-9513
DOI:10.1016/j.ympev.2016.12.033