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- W2170352114 abstract "Full length cDNA sequence of RING domain ubiquitin protein ligase gene TaZFP-1 was acquired by RT-PCR methods. Then, analysis and prediction on the acquired sequences and its amino acids, physicochemical properties, hydrophobicity/hydrophilicity, secondary structure, functional domains, sequence alignment and phylogenetic tree. The results showed that TaZFP-1 gene cDNA was 759 bp in length, encoding 252 amino acids. Most amino acids in TaZFP-1 protein are hydrophilic amino acids, so the protein may be a soluble protein. Secondary structure of TaZFP-1 was mainly composed of a-helices and random coils. Functional domains analysis indicated that the TaZFP-1 is a RING finger domain protein and containing a C3HC4 motif. The molecular evolution threes showed that the TaZFP-1 was clustered into the monocotyledon group and high genetic relationship with O. sativa RING domain E3 ligases." @default.
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- W2170352114 date "2011-06-02" @default.
- W2170352114 modified "2023-10-17" @default.
- W2170352114 title "Cloning and Sequence Analysis of a Wheat RING Domain Ubiquitin Protein Ligase Gene" @default.
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- W2170352114 doi "https://doi.org/10.5539/mas.v5n3p164" @default.
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