node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CG13630 | Galphai | FBpp0084120 | FBpp0076643 | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | G protein alpha i subunit; Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Plays a role in glial cell differentiation during embryogenesis; loco, Galphao and the G-protein coupled receptor, moody, are required in the surface glia to achieve effective insulation of the nerve cord; Belongs to the G-alpha family. G(i/o/t/z) subfamily. | 0.750 |
CG13630 | LeuRS | FBpp0084120 | FBpp0311704 | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Leucyl-tRNA synthetase, isoform A; leucine-tRNA ligase activity; ATP binding; aminoacyl-tRNA editing activity. It is involved in the biological process described with: leucyl-tRNA aminoacylation; wound healing; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.441 |
CG13630 | Nmt | FBpp0084120 | FBpp0076451 | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Glycylpeptide N-tetradecanoyltransferase; Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. | 0.813 |
CG13630 | eEF2 | FBpp0084120 | FBpp0305182 | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity); Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF [...] | 0.735 |
CG13630 | und | FBpp0084120 | FBpp0079462 | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | 0.933 |
CG5188 | LeuRS | FBpp0079614 | FBpp0311704 | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Leucyl-tRNA synthetase, isoform A; leucine-tRNA ligase activity; ATP binding; aminoacyl-tRNA editing activity. It is involved in the biological process described with: leucyl-tRNA aminoacylation; wound healing; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.430 |
CG5188 | Nmt | FBpp0079614 | FBpp0076451 | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Glycylpeptide N-tetradecanoyltransferase; Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. | 0.752 |
CG5188 | eEF2 | FBpp0079614 | FBpp0305182 | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity); Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF [...] | 0.749 |
CG5188 | und | FBpp0079614 | FBpp0079462 | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | 0.838 |
Galphai | CG13630 | FBpp0076643 | FBpp0084120 | G protein alpha i subunit; Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Plays a role in glial cell differentiation during embryogenesis; loco, Galphao and the G-protein coupled receptor, moody, are required in the surface glia to achieve effective insulation of the nerve cord; Belongs to the G-alpha family. G(i/o/t/z) subfamily. | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | 0.750 |
Galphai | Nmt | FBpp0076643 | FBpp0076451 | G protein alpha i subunit; Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Plays a role in glial cell differentiation during embryogenesis; loco, Galphao and the G-protein coupled receptor, moody, are required in the surface glia to achieve effective insulation of the nerve cord; Belongs to the G-alpha family. G(i/o/t/z) subfamily. | Glycylpeptide N-tetradecanoyltransferase; Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. | 0.794 |
Galphai | und | FBpp0076643 | FBpp0079462 | G protein alpha i subunit; Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Plays a role in glial cell differentiation during embryogenesis; loco, Galphao and the G-protein coupled receptor, moody, are required in the surface glia to achieve effective insulation of the nerve cord; Belongs to the G-alpha family. G(i/o/t/z) subfamily. | Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | 0.779 |
LeuRS | CG13630 | FBpp0311704 | FBpp0084120 | Leucyl-tRNA synthetase, isoform A; leucine-tRNA ligase activity; ATP binding; aminoacyl-tRNA editing activity. It is involved in the biological process described with: leucyl-tRNA aminoacylation; wound healing; Belongs to the class-I aminoacyl-tRNA synthetase family. | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | 0.441 |
LeuRS | CG5188 | FBpp0311704 | FBpp0079614 | Leucyl-tRNA synthetase, isoform A; leucine-tRNA ligase activity; ATP binding; aminoacyl-tRNA editing activity. It is involved in the biological process described with: leucyl-tRNA aminoacylation; wound healing; Belongs to the class-I aminoacyl-tRNA synthetase family. | Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | 0.430 |
LeuRS | LeuRS-m | FBpp0311704 | FBpp0073204 | Leucyl-tRNA synthetase, isoform A; leucine-tRNA ligase activity; ATP binding; aminoacyl-tRNA editing activity. It is involved in the biological process described with: leucyl-tRNA aminoacylation; wound healing; Belongs to the class-I aminoacyl-tRNA synthetase family. | Leucyl-tRNA synthetase, mitochondrial; aminoacyl-tRNA editing activity; leucine-tRNA ligase activity; ATP binding. It is involved in the biological process described with: leucyl-tRNA aminoacylation; mitochondrial translation; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.937 |
LeuRS | Nmt | FBpp0311704 | FBpp0076451 | Leucyl-tRNA synthetase, isoform A; leucine-tRNA ligase activity; ATP binding; aminoacyl-tRNA editing activity. It is involved in the biological process described with: leucyl-tRNA aminoacylation; wound healing; Belongs to the class-I aminoacyl-tRNA synthetase family. | Glycylpeptide N-tetradecanoyltransferase; Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. | 0.679 |
LeuRS | eEF2 | FBpp0311704 | FBpp0305182 | Leucyl-tRNA synthetase, isoform A; leucine-tRNA ligase activity; ATP binding; aminoacyl-tRNA editing activity. It is involved in the biological process described with: leucyl-tRNA aminoacylation; wound healing; Belongs to the class-I aminoacyl-tRNA synthetase family. | Elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity); Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF [...] | 0.792 |
LeuRS | und | FBpp0311704 | FBpp0079462 | Leucyl-tRNA synthetase, isoform A; leucine-tRNA ligase activity; ATP binding; aminoacyl-tRNA editing activity. It is involved in the biological process described with: leucyl-tRNA aminoacylation; wound healing; Belongs to the class-I aminoacyl-tRNA synthetase family. | Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | 0.432 |
LeuRS-m | LeuRS | FBpp0073204 | FBpp0311704 | Leucyl-tRNA synthetase, mitochondrial; aminoacyl-tRNA editing activity; leucine-tRNA ligase activity; ATP binding. It is involved in the biological process described with: leucyl-tRNA aminoacylation; mitochondrial translation; Belongs to the class-I aminoacyl-tRNA synthetase family. | Leucyl-tRNA synthetase, isoform A; leucine-tRNA ligase activity; ATP binding; aminoacyl-tRNA editing activity. It is involved in the biological process described with: leucyl-tRNA aminoacylation; wound healing; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.937 |
LeuRS-m | Nmt | FBpp0073204 | FBpp0076451 | Leucyl-tRNA synthetase, mitochondrial; aminoacyl-tRNA editing activity; leucine-tRNA ligase activity; ATP binding. It is involved in the biological process described with: leucyl-tRNA aminoacylation; mitochondrial translation; Belongs to the class-I aminoacyl-tRNA synthetase family. | Glycylpeptide N-tetradecanoyltransferase; Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. | 0.667 |