Since the SPOUT superfamily was defined by homology between the SpoU and TrmD families [Anantharaman, V. et al., J. Mol. Microbiol. Biotechnol., 4, 71-75 (2002)], many crystal structures have been solved and numerous new homologous sequences have been found in the superfamily. Therefore, nowadays, we can consider enzyme function and/or evolution process of the SPOUT superfamily members using not only amino acid sequences but also protein structures. Recently, a bioinformatics research on SPOUT superfamily proposed existences of new member proteins [COG1756, COG1772, COG4080, and COG1901], and provided a structural and evolutionary classification of the proteins [Tkaczuk, K.L. et al., BMC Bioinformatics, 8:73 (2007)], which serves as a guide for studies on the SPOUT family in future. In this meeting, we report a new approach using a flexible protein structure alignment algorithm (FATCAT) to analyze the structures of SPOUT superfamily proteins, and discuss differences in substrate selectivities of methyltransferases in the superfamily.
Differences in substrate selectivities of the SPOUT superfamily of methyltransferases. Publishing Authors By Initials
Differences in substrate selectivities of the SPOUT superfamily of methyltransferases. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Nucleic acids symposium series (2004)
VOLUME:
Page Numbers: 445-6
Journal Abbreviation: Nucleic Acids Symp Ser (Oxf)
ISSN: 1746-8272
DAY: 21
MONTH: 11
YEAR: 2007
Differences in substrate selectivities of the SPOUT superfamily of methyltransferases. Information
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LANGUAGE: eng
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Grant and Affiliation Information for Differences in substrate selectivities of the SPOUT superfamily of methyltransferases.
AFFILIATION: Department of Materials Science and Biotechnology, Graduate School of Science and Engineering Ehime University, Bunkyo 3 Matuyama 790-8577, Japan.
Country: England
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MEDLINETA: Nucleic Acids Symp Ser (Oxf)
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