EOG82C0R8	GO:0008168	24/85	methyltransferase activity	molecular_function	"Catalysis of the transfer of a methyl group to an acceptor molecule." [ISBN:0198506732]
EOG82C0R8	GO:0018016	1/85	N-terminal peptidyl-proline dimethylation	biological_process	"The methylation of the N-terminal proline of proteins to form the derivative N,N-dimethyl-L-proline." [RESID:AA0066]
EOG82C0R8	GO:0016571	1/85	histone methylation	biological_process	"The modification of histones by addition of methyl groups." [GOC:ai]
EOG82C0R8	GO:0035568	1/85	N-terminal peptidyl-proline methylation	biological_process	"The methylation of the N-terminal proline of proteins." [PMID:20668449, RESID:AA0419]
EOG82C0R8	GO:0000179	1/85	rRNA (adenine-N6,N6-)-dimethyltransferase activity	molecular_function	"Catalysis of the dimethylation two adjacent A residues in the loop closing the 3'-terminal stem of the 18S rRNA, using S-adenosyl-L-methionine as a methyl donor." [ISBN:1555811337, PMID:10690410]
EOG82C0R8	GO:0005634	1/85	nucleus	cellular_component	"A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent." [GOC:go_curators]
EOG82C0R8	GO:0071885	1/85	N-terminal protein N-methyltransferase activity	molecular_function	"Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the alpha-amino group of the N-terminal amino or imino acid residue of a protein substrate. For example, yeast Tae1p and mammalian family member METTL11A preferentially modify the N-terminal residue of substrates with the N-terminal sequence X-Pro-Lys, where X can be Pro, Ala, or Ser." [PMID:20481588]
EOG82C0R8	GO:0042054	1/85	histone methyltransferase activity	molecular_function	"Catalysis of the reaction: S-adenosyl-L-methionine + histone = S-adenosyl-L-homocysteine + methyl-histone. Histone methylation generally occurs on either an arginine or lysine residue." [EC:2.1.1.43]