| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KXA30502.1 | KXA30506.1 | HMPREF3229_00965 | HMPREF3229_00969 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Thioesterase family protein; KEGG: hhd:HBHAL_4546 1.7e-21 cytosolic long-chain acyl-CoA thioester hydrolase family protein; Psort location: Cytoplasmic, score: 7.50. | 0.691 |
| KXA30502.1 | map | HMPREF3229_00965 | HMPREF3229_00963 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Methionine aminopeptidase, type I; 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.790 |
| KXA30502.1 | psuG | HMPREF3229_00965 | HMPREF3229_00968 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Indigoidine synthase A-like protein; Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway; Belongs to the pseudouridine-5'-phosphate glycosidase family. | 0.624 |
| KXA30502.1 | psuK | HMPREF3229_00965 | HMPREF3229_00967 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | HTH domain protein; KEGG: cbj:H04402_01237 3.1e-70 pseudouridine kinase; Psort location: Cytoplasmic, score: 7.50. | 0.704 |
| KXA30502.1 | tdk | HMPREF3229_00965 | HMPREF3229_00966 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Thymidine kinase; KEGG: fma:FMG_0715 1.9e-54 thymidine kinase; K00857 thymidine kinase; Psort location: Cytoplasmic, score: 9.97. | 0.804 |
| KXA30506.1 | KXA30502.1 | HMPREF3229_00969 | HMPREF3229_00965 | Thioesterase family protein; KEGG: hhd:HBHAL_4546 1.7e-21 cytosolic long-chain acyl-CoA thioester hydrolase family protein; Psort location: Cytoplasmic, score: 7.50. | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.691 |
| KXA30506.1 | map | HMPREF3229_00969 | HMPREF3229_00963 | Thioesterase family protein; KEGG: hhd:HBHAL_4546 1.7e-21 cytosolic long-chain acyl-CoA thioester hydrolase family protein; Psort location: Cytoplasmic, score: 7.50. | Methionine aminopeptidase, type I; 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.622 |
| KXA30506.1 | psuG | HMPREF3229_00969 | HMPREF3229_00968 | Thioesterase family protein; KEGG: hhd:HBHAL_4546 1.7e-21 cytosolic long-chain acyl-CoA thioester hydrolase family protein; Psort location: Cytoplasmic, score: 7.50. | Indigoidine synthase A-like protein; Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway; Belongs to the pseudouridine-5'-phosphate glycosidase family. | 0.773 |
| KXA30506.1 | psuK | HMPREF3229_00969 | HMPREF3229_00967 | Thioesterase family protein; KEGG: hhd:HBHAL_4546 1.7e-21 cytosolic long-chain acyl-CoA thioester hydrolase family protein; Psort location: Cytoplasmic, score: 7.50. | HTH domain protein; KEGG: cbj:H04402_01237 3.1e-70 pseudouridine kinase; Psort location: Cytoplasmic, score: 7.50. | 0.789 |
| KXA30506.1 | tdk | HMPREF3229_00969 | HMPREF3229_00966 | Thioesterase family protein; KEGG: hhd:HBHAL_4546 1.7e-21 cytosolic long-chain acyl-CoA thioester hydrolase family protein; Psort location: Cytoplasmic, score: 7.50. | Thymidine kinase; KEGG: fma:FMG_0715 1.9e-54 thymidine kinase; K00857 thymidine kinase; Psort location: Cytoplasmic, score: 9.97. | 0.660 |
| apeB | psuG | HMPREF3229_01475 | HMPREF3229_00968 | Aspartyl aminopeptidase domain protein; KEGG: apv:Apar_0506 5.9e-124 putative aminopeptidase 2; Psort location: Cytoplasmic, score: 7.50. | Indigoidine synthase A-like protein; Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway; Belongs to the pseudouridine-5'-phosphate glycosidase family. | 0.865 |
| codA | pdp | HMPREF3229_01171 | HMPREF3229_00785 | Putative cytosine deaminase; KEGG: aur:HMPREF9243_0572 1.6e-153 codA; cytosine deaminase K01485; Psort location: Cytoplasmic, score: 7.50. | KEGG: tna:CTN_0734 7.6e-115 Pyrimidine-nucleoside phosphorylase; K00756 pyrimidine-nucleoside phosphorylase. | 0.918 |
| codA | psuG | HMPREF3229_01171 | HMPREF3229_00968 | Putative cytosine deaminase; KEGG: aur:HMPREF9243_0572 1.6e-153 codA; cytosine deaminase K01485; Psort location: Cytoplasmic, score: 7.50. | Indigoidine synthase A-like protein; Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway; Belongs to the pseudouridine-5'-phosphate glycosidase family. | 0.900 |
| codA | punA | HMPREF3229_01171 | HMPREF3229_00784 | Putative cytosine deaminase; KEGG: aur:HMPREF9243_0572 1.6e-153 codA; cytosine deaminase K01485; Psort location: Cytoplasmic, score: 7.50. | Purine nucleoside phosphorylase I, inosine and guanosine-specific; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.923 |
| codA | upp | HMPREF3229_01171 | HMPREF3229_01417 | Putative cytosine deaminase; KEGG: aur:HMPREF9243_0572 1.6e-153 codA; cytosine deaminase K01485; Psort location: Cytoplasmic, score: 7.50. | Uracil phosphoribosyltransferase; Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate. | 0.930 |
| map | KXA30502.1 | HMPREF3229_00963 | HMPREF3229_00965 | Methionine aminopeptidase, type I; 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.790 |
| map | KXA30506.1 | HMPREF3229_00963 | HMPREF3229_00969 | Methionine aminopeptidase, type I; 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Thioesterase family protein; KEGG: hhd:HBHAL_4546 1.7e-21 cytosolic long-chain acyl-CoA thioester hydrolase family protein; Psort location: Cytoplasmic, score: 7.50. | 0.622 |
| map | psuG | HMPREF3229_00963 | HMPREF3229_00968 | Methionine aminopeptidase, type I; 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Indigoidine synthase A-like protein; Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway; Belongs to the pseudouridine-5'-phosphate glycosidase family. | 0.606 |
| map | psuK | HMPREF3229_00963 | HMPREF3229_00967 | Methionine aminopeptidase, type I; 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | HTH domain protein; KEGG: cbj:H04402_01237 3.1e-70 pseudouridine kinase; Psort location: Cytoplasmic, score: 7.50. | 0.612 |
| map | tdk | HMPREF3229_00963 | HMPREF3229_00966 | Methionine aminopeptidase, type I; 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Thymidine kinase; KEGG: fma:FMG_0715 1.9e-54 thymidine kinase; K00857 thymidine kinase; Psort location: Cytoplasmic, score: 9.97. | 0.759 |
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