node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EFM5 | EFM6 | F7VVE1 | F7W4K1 | Protein-lysine N-methyltransferase EFM5; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that trimethylates elongation factor 1-alpha at 'Lys- 79'; Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM5 family. | Protein-lysine N-methyltransferase EFM6; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that methylates elongation factor 1-alpha. Belongs to the class I-like SAM-binding methyltransferase superfamily. METTL21 family. EFM6 subfamily. | 0.447 |
EFM5 | SMAC_01918 | F7VVE1 | F7VS86 | Protein-lysine N-methyltransferase EFM5; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that trimethylates elongation factor 1-alpha at 'Lys- 79'; Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM5 family. | WGS project CABT00000000 data, contig 2.5. | 0.627 |
EFM6 | EFM5 | F7W4K1 | F7VVE1 | Protein-lysine N-methyltransferase EFM6; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that methylates elongation factor 1-alpha. Belongs to the class I-like SAM-binding methyltransferase superfamily. METTL21 family. EFM6 subfamily. | Protein-lysine N-methyltransferase EFM5; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that trimethylates elongation factor 1-alpha at 'Lys- 79'; Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM5 family. | 0.447 |
EFM6 | EFM7 | F7W4K1 | F7VW32 | Protein-lysine N-methyltransferase EFM6; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that methylates elongation factor 1-alpha. Belongs to the class I-like SAM-binding methyltransferase superfamily. METTL21 family. EFM6 subfamily. | Protein N-terminal and lysine N-methyltransferase EFM7; S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono-and dimethylation of 'Lys-3'. Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM7 family. | 0.416 |
EFM6 | SMAC_01918 | F7W4K1 | F7VS86 | Protein-lysine N-methyltransferase EFM6; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that methylates elongation factor 1-alpha. Belongs to the class I-like SAM-binding methyltransferase superfamily. METTL21 family. EFM6 subfamily. | WGS project CABT00000000 data, contig 2.5. | 0.649 |
EFM6 | SMAC_03408 | F7W4K1 | F7VW30 | Protein-lysine N-methyltransferase EFM6; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that methylates elongation factor 1-alpha. Belongs to the class I-like SAM-binding methyltransferase superfamily. METTL21 family. EFM6 subfamily. | Putative copper-regulated transcription factor. | 0.416 |
EFM7 | EFM6 | F7VW32 | F7W4K1 | Protein N-terminal and lysine N-methyltransferase EFM7; S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono-and dimethylation of 'Lys-3'. Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM7 family. | Protein-lysine N-methyltransferase EFM6; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that methylates elongation factor 1-alpha. Belongs to the class I-like SAM-binding methyltransferase superfamily. METTL21 family. EFM6 subfamily. | 0.416 |
EFM7 | SMAC_01918 | F7VW32 | F7VS86 | Protein N-terminal and lysine N-methyltransferase EFM7; S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono-and dimethylation of 'Lys-3'. Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM7 family. | WGS project CABT00000000 data, contig 2.5. | 0.454 |
SMAC_00007 | SMAC_05004 | F7VJW5 | F7VUP9 | WGS project CABT00000000 data, contig 2.1. | WGS project CABT00000000 data, contig 2.8. | 0.420 |
SMAC_00007 | SMAC_06682 | F7VJW5 | F7VYB6 | WGS project CABT00000000 data, contig 2.1. | WGS project CABT00000000 data, contig 2.13; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily. | 0.533 |
SMAC_00083 | SMAC_00488 | F7VK40 | F7VL94 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. | WGS project CABT00000000 data, contig 2.1. | 0.922 |
SMAC_00083 | SMAC_03785 | F7VK40 | F7VZX9 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. | WGS project CABT00000000 data, contig 2.16. | 0.592 |
SMAC_00083 | SMAC_05383 | F7VK40 | F7VSS5 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. | WGS project CABT00000000 data, contig 2.6. | 0.941 |
SMAC_00083 | SMAC_06682 | F7VK40 | F7VYB6 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. | WGS project CABT00000000 data, contig 2.13; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily. | 0.967 |
SMAC_00083 | SMAC_07345 | F7VK40 | F7W8J1 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. | WGS project CABT00000000 data, contig 2.45. | 0.917 |
SMAC_00083 | SMAC_07534 | F7VK40 | F7VTR0 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. | WGS project CABT00000000 data, contig 2.7. | 0.974 |
SMAC_00083 | SMAC_08061 | F7VK40 | F7W9B4 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. | WGS project CABT00000000 data, contig 2.50. | 0.477 |
SMAC_00083 | SMAC_08815 | F7VK40 | F7WAW1 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. | WGS project CABT00000000 data, contig 2.66. | 0.944 |
SMAC_00488 | SMAC_00083 | F7VL94 | F7VK40 | WGS project CABT00000000 data, contig 2.1. | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. | 0.922 |
SMAC_00488 | SMAC_05004 | F7VL94 | F7VUP9 | WGS project CABT00000000 data, contig 2.1. | WGS project CABT00000000 data, contig 2.8. | 0.438 |