A highly conserved family of domains related to the DNA-glycosylase fold helps predict multiple novel pathways for RNA modifications

RNA Biology

Volumn 11, Issue 4, 2014, Pages 360-372

  Maxwell Burroughs, A ^a   Aravind, L ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

Base modification; Caliban; DNA glycosylase; FbpA; Fibronectin binding; IscS; NEMF; Tae2; TRNA 4 thiouridylation; TusA

Indexed keywords

DNA GLYCOSYLTRANSFERASE; DOUBLE STRANDED RNA; ENZYME; PYRIMIDINE DERIVATIVE; SULFUR; TRANSFER RNA; RNA;

ARCHAEON; ARTICLE; DROSOPHILA; EUKARYOTE; GENOME; MULTIGENE FAMILY; NONHUMAN; PHYLOGENY; PROKARYOTE; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION; RNA BINDING; AMINO ACID SEQUENCE; ANIMAL; BIOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ANIMALS; COMPUTATIONAL BIOLOGY; CONSERVED SEQUENCE; DNA GLYCOSYLASES; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; RNA; SEQUENCE ALIGNMENT;

EID: 84901462090     PISSN: 15476286     EISSN: 15558584     Source Type: Journal    
DOI: 10.4161/rna.28302     Document Type: Article

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