Trm13p, the tRNA:Xm4 modification enzyme from Saccharomyces cerevisiae is a member of the Rossmann-fold MTase superfamily: Prediction of structure and active site

Journal of Molecular Modeling

Volumn 16, Issue 3, 2010, Pages 599-606

  Tkaczuk, Karolina L ^a,b  

^a INTERNATIONAL INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Poland)

^b LODZ UNIVERSITY OF TECHNOLOGY   (Poland)

Author keywords

Methyltransferase; Protein fold recognition; RNA modification; Rossmann fold methyltransferase; Zn finger domain

Indexed keywords

FIBRILLARIN; PROTEIN TRM13P; RNA METHYLTRANSFERASE; TRANSFER RNA; UNCLASSIFIED DRUG; CYSTEINE; HISTIDINE; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSFER RNA METHYLTRANSFERASE; TRM13 PROTEIN, S CEREVISIAE;

AMINO ACID SEQUENCE; ARTICLE; BIOINFORMATICS; ENZYME ACTIVE SITE; ENZYME MODIFICATION; ENZYME STRUCTURE; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN METHYLATION; PROTEIN MOTIF; SACCHAROMYCES CEREVISIAE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT;

EUKARYOTA; SACCHAROMYCES CEREVISIAE;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CYSTEINE; HISTIDINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; RNA, TRANSFER; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; TRNA METHYLTRANSFERASES;

EID: 77951219636     PISSN: 16102940     EISSN: 09485023     Source Type: Journal    
DOI: 10.1007/s00894-009-0570-6     Document Type: Article

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