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Figure 7 | BMC Genomics

Figure 7

From: The RST and PARP-like domain containing SRO protein family: analysis of protein structure, function and conservation in land plants

Figure 7

The RST domain of the plant SRO protein family contains a strongly conserved amino acid pattern. (A) Domain structure of AtRCD1 and TAF4s from multiple species (Saccharomyces cerevisiae, Schizosaccharomyces pombe, Homo sapiens, Drosophila melanogaster). All TAF4s have the conserved TAF4 superfamily domain (TAF4; PF05236). Yeast TAF4s lack an N-terminal extension while metazoan TAF4s have an extension bearing an ETO domain (ETO/TAFH domain; PF07531), which is a known transcription factor-recruitment domain [43]. Plant TAF4s also have an N-terminal extension that lacks the ETO domain but bears the structurally unrelated plant-specific RST (RCD1-SRO-TAF4; PF12174) domain. TAF4 RST has not been tested for TF interaction, however, the RST domain from AtRCD1 is required for interaction with multiple TFs. AtRCD1 also bears PARP-like (PS51059) and WWE (PS50918) domains. (B) The C-terminal RST domain of the different groups and subgroups (Ia, Ib, Ic, IIa, IIb) of the plant SRO protein family were aligned using ClustalW and Boxshade. Consensus sequences for each group or subgroup are depicted in bold characters and marked according to similarity: conserved (*), strong similarty (:), weak similarity (.) using Boxshade. Under the sequence, alternatives for AAs are shown. AAs with similar chemical properties are indicated using colored bars. Green indicates polar, non-charged, non-aliphatic residues. Blue indicates the most hydrophobic AAs. Red indicates positively charged AAs. Magenta highlights acidic residues. Orange shows glycine and brown indicates tyrosine.

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