EC Number   |
General Information |
Reference |
|---|
   2.1.1.244 | evolution |
enzymatic functional conservation of NRMT1 across species, evolutionary conservation of histone alpha-N-modification. Coevolution of NRMT1 recognition motifs in RCC1, CENP-A, and CENP-B, in which sequences 1SPKRIA6 of RCC1, 1GPRRRS6 of CENP-A, and 1GPKRRQ6 of CENP-B co-occur in mammals but are all missing in lower organisms. In contrast, the NRMT1 recognition motif of histone H2B is conserved from ciliates to insects but is lost in mammals. Remarkably, yeast and chicken orthologues of the above proteins do not harbor an NRMT1 recognition motif, suggesting that NRMT1 may exert its cellular function in these organisms through other protein substrates |
756877 |
| 2.1.1.244 | evolution |
enzyme Efm5 is a distinct type of eukaryotic N-terminal methyltransferase as, unlike the three other known eukaryotic N-terminal methyltransferases, its substrate does not have an N-terminal [A/P/S]-P-K motif. The N-terminal methylation of eEF1A is also present in human catalyzed by enzyme N6AMT2, this conservation over a large evolutionary distance suggests it to be of functional importance. The trimethylation of Lys79 in eEF1A is conserved from yeast to human. Human enzyme N6AMT2 is the direct orthologue of the yeast Efm5, and Efm5 and N6AMT2 can methylate eEF1A from either species in vitro |
-, 757664 |
| 2.1.1.244 | evolution |
METTL11a, i.e. NRMT, encodes a 25 kDa protein in the methyltransferase 11 family, most members of which methylate metabolites or other small molecules. alpha-N-methyltransferase is a conserved member of a superfamily of non-SET domain enzymes |
718160 |
| 2.1.1.244 | evolution |
Rkm2 belongs to the SET domain methyltransferases |
-, 717778 |
| 2.1.1.244 | evolution |
structural comparison of isozymes NTMT1 and NTMT2 (EC 2.1.1.299), overview. NTMT1 and NTMT2 employ a similar substrate recognition mode |
756502 |
| 2.1.1.244 | evolution |
the enzyme belongs to the methyltransferase like (METTL) family of class I methyltransferases containing seven-beta-strand methyltransferase motifs and Rossman folds for binding SAM. The N-terminal methyltransferase homologs NRMT1 (N-terminal RCC1 methyltransferase 1) and NRMT2 (N-terminal RCC1 methyltransferase 2), which following cleavage of the initiating methionine, methylate the alpha-amine of the first N-terminal residue of their substrates. NRMT1 and NRMT2 are 50% identical and 75% similar and share an N-terminal X-P-K consensus sequence. Although structurally similar, they differ in their catalytic activities |
758296 |
| 2.1.1.244 | evolution |
the enzyme is a distinct type of eukaryotic N-terminal methyltransferase as, unlike the three other known eukaryotic N-terminal methyltransferases, its substrate does not have an N-terminal [A/P/S]-P-K motif. The N-terminal methylation of eEF1A is also present in yeast catalyzed by enzymes Efm5 and Efm7, this conservation over a large evolutionary distance suggests it to be of functional importance. The trimethylation of Lys79 in eEF1A is conserved from yeast to human. Human enzyme N6AMT2 is the direct orthologue of the yeast Efm5, and Efm5 and N6AMT2 can methylate eEF1A from either species in vitro. Methyltransferases that act on lysine 79 in eEF1A are conserved from yeast to human |
757664 |
| 2.1.1.244 | evolution |
YLR285W is termed elongation factor methyltransferase 7 (Efm7). This enzyme is a distinct type of eukaryotic N-terminal methyltransferase as, unlike the three other known eukaryotic N-terminal methyltransferases, its substrate does not have an N-terminal [A/P/S]-P-K motif. The N-terminal methylation of eEF1A is also present in human catalyzed by enzyme N6AMT2, this conservation over a large evolutionary distance suggests it to be of functional importance. The trimethylation of Lys79 in eEF1A is conserved from yeast to human |
-, 757664 |
| 2.1.1.244 | malfunction |
aberrant N-terminal methylation has been implicated in several cancers and developmental diseases |
756441 |
| 2.1.1.244 | malfunction |
deletion of YBR261C in yeast abolishes N-terminal methylation, which consequently alters the ribosomal profile and leads to defects in both translational efficiency and fidelity. Overexpression of YBR261 validates its involvement in protein synthesis |
-, 756463 |
