| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Tpet_1232 | Tpet_1234 | Tpet_1232 | Tpet_1234 | PFAM: Formiminotransferase-cyclodeaminase. | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region. | 0.818 |
| Tpet_1232 | Tpet_1235 | Tpet_1232 | Tpet_1235 | PFAM: Formiminotransferase-cyclodeaminase. | PFAM: helix-hairpin-helix motif; DNA repair protein RadC; Belongs to the UPF0758 family. | 0.769 |
| Tpet_1232 | Tpet_1236 | Tpet_1232 | Tpet_1236 | PFAM: Formiminotransferase-cyclodeaminase. | Maf protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | 0.769 |
| Tpet_1232 | Tpet_1237 | Tpet_1232 | Tpet_1237 | PFAM: Formiminotransferase-cyclodeaminase. | PFAM: Heptaprenyl diphosphate synthase component I. | 0.739 |
| Tpet_1232 | Tpet_1238 | Tpet_1232 | Tpet_1238 | PFAM: Formiminotransferase-cyclodeaminase. | PFAM: protein of unknown function DUF1312. | 0.735 |
| Tpet_1232 | Tpet_1239 | Tpet_1232 | Tpet_1239 | PFAM: Formiminotransferase-cyclodeaminase. | ApbE family lipoprotein; Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein. | 0.768 |
| Tpet_1232 | Tpet_1240 | Tpet_1232 | Tpet_1240 | PFAM: Formiminotransferase-cyclodeaminase. | PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB. | 0.732 |
| Tpet_1232 | Tpet_1241 | Tpet_1232 | Tpet_1241 | PFAM: Formiminotransferase-cyclodeaminase. | PFAM: AMMECR1 domain protein. | 0.716 |
| Tpet_1232 | deoC | Tpet_1232 | Tpet_1233 | PFAM: Formiminotransferase-cyclodeaminase. | Deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate; Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily. | 0.821 |
| Tpet_1232 | tgt | Tpet_1232 | Tpet_1231 | PFAM: Formiminotransferase-cyclodeaminase. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). 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, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form th [...] | 0.826 |
| Tpet_1234 | Tpet_1232 | Tpet_1234 | Tpet_1232 | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region. | PFAM: Formiminotransferase-cyclodeaminase. | 0.818 |
| Tpet_1234 | Tpet_1235 | Tpet_1234 | Tpet_1235 | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region. | PFAM: helix-hairpin-helix motif; DNA repair protein RadC; Belongs to the UPF0758 family. | 0.778 |
| Tpet_1234 | Tpet_1236 | Tpet_1234 | Tpet_1236 | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region. | Maf protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | 0.778 |
| Tpet_1234 | Tpet_1237 | Tpet_1234 | Tpet_1237 | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region. | PFAM: Heptaprenyl diphosphate synthase component I. | 0.778 |
| Tpet_1234 | Tpet_1238 | Tpet_1234 | Tpet_1238 | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region. | PFAM: protein of unknown function DUF1312. | 0.749 |
| Tpet_1234 | Tpet_1239 | Tpet_1234 | Tpet_1239 | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region. | ApbE family lipoprotein; Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein. | 0.777 |
| Tpet_1234 | Tpet_1240 | Tpet_1234 | Tpet_1240 | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region. | PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB. | 0.745 |
| Tpet_1234 | Tpet_1241 | Tpet_1234 | Tpet_1241 | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region. | PFAM: AMMECR1 domain protein. | 0.730 |
| Tpet_1234 | deoC | Tpet_1234 | Tpet_1233 | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region. | Deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate; Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily. | 0.811 |
| Tpet_1234 | tgt | Tpet_1234 | Tpet_1231 | TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region. | Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). 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, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form th [...] | 0.818 |