| Ensembl ID | Symbol | Entrez ID | RBD | RBPome | PRI | Expresion | Pathway | Phenotype | Paralog | Ortholog | GO |
|---|---|---|---|---|---|---|---|---|---|---|---|
The function of this family is uncertain. The bacterial members are about 60-70 amino acids in length and the eukaryotic examples are about 120 amino acids in length. The C terminus contains the strongest conservation. Trm112p is required for tRNA methylation in S. cerevisiae and is found in complexes with 2 tRNA methylases (TRM9 and TRM11) also with putative methyltransferase YDR140W [1]. The zinc-finger protein Ynr046w is plurifunctional and a component of the eRF1 methyltransferase in yeast [2]. The crystal structure of Ynr046w has been determined to 1.7 A resolution. It comprises a zinc-binding domain built from both the N- and C-terminal sequences and an inserted domain, absent from bacterial and archaeal orthologs of the protein, composed of three alpha-helices [2].
The function of this family is uncertain. The bacterial members are about 60-70 amino acids in length and the eukaryotic examples are about 120 amino acids in length. The C terminus contains the strongest conservation. The entry contains:
Purushothaman SK, Bujnicki JM, Grosjean H, Lapeyre B; , Mol Cell Biol 2005;25:4359-4370.: Trm11p and Trm112p Are both Required for the Formation of 2-Methylguanosine at Position 10 in Yeast tRNA. PUBMED:15899842 EPMC:15899842 .
Heurgue-Hamard V, Graille M, Scrima N, Ulryck N, Champ S, van Tilbeurgh H, Buckingham RH; , J Biol Chem. 2006;281:36140-36148.: The zinc finger protein Ynr046w is plurifunctional and a component of the eRF1 methyltransferase in yeast. PUBMED:17008308 EPMC:17008308.
