Abstract (1zkd)
Abstract
Although the human genome has been revealed the actual proteome remains poorly understood as there are a lot of unknown proteins and known proteins with unknown function. Data from proteomic research centers using high throughput methods are publicly available and though a lot of structures of unknown proteins have been identified, no further analysis has been made to reveal the actual functional and evolutional background of the proteins. In this study we investigate the unknown hypothetical protein LOC55471 isoform 1 by using a variety of bioinformatic tools and by datamining of publicly available databases. Most information were taken from the known structure of the bacterial protein from Rhodopseudomonas palustris to get information about the possible structure, function and evolution of the mouse and human orthologs. Structural and functional analysis revealed similarities to a higher number of s-adenosylmethionine dependent methyltransferases from bacteria and human and the lack of nuclear localisation signals indicates that LOC55471 isoform 1 might be a putative methyltransferase acting in the cytoplasm or in mitochondria. As methylation of proteins and nucleic acids like RNA plays an important role in a lot of cellular processes we present here a putative new player in the field of posttranslational and posttranscriptional modification.
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