ArticleBioinformation2019
Annotation of a hypothetical protein coding gene PAS_chr2-2_0152 containing Lysine Methyl transferase SMYD domain from Komagataella phaffii GS115.
Article in Bioinformation, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 1 citations in OpenAlex.
- Structure based functional annotation of a MYND-less lysine methyl transferase inBioinformation · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The methylotrophic yeast Komagataella phaffii is an industrial workhorse yeast species that has been widely used in biotechnology industries for recombinant protein production. Genome sequencing of this yeast in 2009 have enabled scientists to assign and characterize functions to most of its proteins while few hypothetical proteins remain uncharacterized. Therefore, it is of interest to characterize the hypothetical protein coding gene PAS_chr2-2_0152 as SET containing the ZNF-MYND (SMYD) domain. They share a homology with other methylotrophic and non-methylotrophic yeast species together with known SMYD proteins of Homo sapiens, with conserved distinctive SMYD domain patterns. A homology model is developed using the crystal structure of human histone-lysine methyl transferase smyd3 as template. These data points to that the hypothetical protein is a potential histones and non-histone lysine methyl transferase regulating cell cycle, chromatin remodeling, DNA damage response, homologous recombination and transcription in Komagataella phaffii. Data also suggests the evolutionary syntenic conservation of DNA damage regulator (RFX) and lysine methyl transferase (SMYD) genes in some yeast lineages, pointing to a conserved role requiring further confirmation.
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