| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| bckdk | nudt22 | ENSDARP00000021993 | ENSDARP00000121110 | Protein-serine/threonine kinase. | Nudix (nucleoside diphosphate-linked moiety X)-type motif 22. | 0.755 |
| bckdk | ostm1 | ENSDARP00000021993 | ENSDARP00000150259 | Protein-serine/threonine kinase. | Osteoclastogenesis-associated transmembrane protein 1. | 0.696 |
| bckdk | qtrt1 | ENSDARP00000021993 | ENSDARP00000063286 | Protein-serine/threonine kinase. | Queuine tRNA-ribosyltransferase catalytic subunit 1; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, formi [...] | 0.757 |
| bckdk | trabd | ENSDARP00000021993 | ENSDARP00000015662 | Protein-serine/threonine kinase. | TraB domain-containing. | 0.433 |
| bckdk | wdyhv1 | ENSDARP00000021993 | ENSDARP00000094043 | Protein-serine/threonine kinase. | Protein N-terminal glutamine amidohydrolase; Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested sec [...] | 0.746 |
| nudt22 | bckdk | ENSDARP00000121110 | ENSDARP00000021993 | Nudix (nucleoside diphosphate-linked moiety X)-type motif 22. | Protein-serine/threonine kinase. | 0.755 |
| nudt22 | ostm1 | ENSDARP00000121110 | ENSDARP00000150259 | Nudix (nucleoside diphosphate-linked moiety X)-type motif 22. | Osteoclastogenesis-associated transmembrane protein 1. | 0.603 |
| nudt22 | qtrt1 | ENSDARP00000121110 | ENSDARP00000063286 | Nudix (nucleoside diphosphate-linked moiety X)-type motif 22. | Queuine tRNA-ribosyltransferase catalytic subunit 1; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, formi [...] | 0.724 |
| nudt22 | trabd | ENSDARP00000121110 | ENSDARP00000015662 | Nudix (nucleoside diphosphate-linked moiety X)-type motif 22. | TraB domain-containing. | 0.750 |
| nudt22 | wdyhv1 | ENSDARP00000121110 | ENSDARP00000094043 | Nudix (nucleoside diphosphate-linked moiety X)-type motif 22. | Protein N-terminal glutamine amidohydrolase; Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested sec [...] | 0.728 |
| ostm1 | bckdk | ENSDARP00000150259 | ENSDARP00000021993 | Osteoclastogenesis-associated transmembrane protein 1. | Protein-serine/threonine kinase. | 0.696 |
| ostm1 | nudt22 | ENSDARP00000150259 | ENSDARP00000121110 | Osteoclastogenesis-associated transmembrane protein 1. | Nudix (nucleoside diphosphate-linked moiety X)-type motif 22. | 0.603 |
| ostm1 | qtrt1 | ENSDARP00000150259 | ENSDARP00000063286 | Osteoclastogenesis-associated transmembrane protein 1. | Queuine tRNA-ribosyltransferase catalytic subunit 1; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, formi [...] | 0.750 |
| ostm1 | trabd | ENSDARP00000150259 | ENSDARP00000015662 | Osteoclastogenesis-associated transmembrane protein 1. | TraB domain-containing. | 0.750 |
| ostm1 | wdyhv1 | ENSDARP00000150259 | ENSDARP00000094043 | Osteoclastogenesis-associated transmembrane protein 1. | Protein N-terminal glutamine amidohydrolase; Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested sec [...] | 0.750 |
| qtrt1 | bckdk | ENSDARP00000063286 | ENSDARP00000021993 | Queuine tRNA-ribosyltransferase catalytic subunit 1; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, formi [...] | Protein-serine/threonine kinase. | 0.757 |
| qtrt1 | nudt22 | ENSDARP00000063286 | ENSDARP00000121110 | Queuine tRNA-ribosyltransferase catalytic subunit 1; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, formi [...] | Nudix (nucleoside diphosphate-linked moiety X)-type motif 22. | 0.724 |
| qtrt1 | ostm1 | ENSDARP00000063286 | ENSDARP00000150259 | Queuine tRNA-ribosyltransferase catalytic subunit 1; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, formi [...] | Osteoclastogenesis-associated transmembrane protein 1. | 0.750 |
| qtrt1 | qtrt2 | ENSDARP00000063286 | ENSDARP00000113635 | Queuine tRNA-ribosyltransferase catalytic subunit 1; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, formi [...] | Queuine tRNA-ribosyltransferase accessory subunit 2; Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine); Belongs to the queuine tRNA-ribosyltransferase family. QTRT2 subfamily. | 0.984 |
| qtrt1 | trabd | ENSDARP00000063286 | ENSDARP00000015662 | Queuine tRNA-ribosyltransferase catalytic subunit 1; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, formi [...] | TraB domain-containing. | 0.750 |