| Ensembl ID | Symbol | Entrez ID | RBD | RBPome | PRI | Expresion | Pathway | Phenotype | Paralog | Ortholog | GO |
|---|---|---|---|---|---|---|---|---|---|---|---|
This family has a TIM barrel-like fold with a deep C-terminal trefoil knot. The arrangement of its hydrophilic and hydrophobic surfaces are opposite to that of the classic TIM barrel proteins. It is likely to bind RNA [1] and may function as a methyltransferase [2,3].
This family has a TIM barrel-like fold with a deep C-terminal trefoil knot. The arrangement of its hydrophilic and hydrophobic surfaces are opposite to that of the classic TIM barrel proteins. It is likely to bind RNA [PUBMED:12486711], and may function as a methyltransferase [PUBMED:17338813, PUBMED:18844986].
Zarembinski TI, Kim Y, Peterson K, Christendat D, Dharamsi A, Arrowsmith CH, Edwards AM, Joachimiak A;, Proteins. 2003;50:177-183.: Deep trefoil knot implicated in RNA binding found in an archaebacterial protein. PUBMED:12486711 EPMC:12486711 .
Tkaczuk KL, Dunin-Horkawicz S, Purta E, Bujnicki JM; , BMC Bioinformatics. 2007;8:73.: Structural and evolutionary bioinformatics of the SPOUT superfamily of methyltransferases. PUBMED:17338813 EPMC:17338813 .
Grosjean H, Gaspin C, Marck C, Decatur WA, de Crecy-Lagard V;, BMC Genomics. 2008;9:470.: RNomics and Modomics in the halophilic archaea Haloferax volcanii: identification of RNA modification genes. PUBMED:18844986 EPMC:18844986.
