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Tint_2667 | KEGG: aav:Aave_3581 serine/threonine protein kinase; PFAM: Serine/threonine-protein kinase-like domain; SMART: serine/threonine protein kinase; Tyrosine-protein kinase, subgroup, catalytic domain. (359 aa) | ||||
Tint_2668 | KEGG: pol:Bpro_1338 protein serine/threonine phosphatases; PFAM: Protein phosphatase 2C-like; SMART: protein phosphatase 2C domain protein. (307 aa) | ||||
rph | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. (243 aa) | ||||
Tint_2670 | Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. (255 aa) | ||||
Tint_2671 | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (429 aa) |
node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Tint_2667 | Tint_2668 | Tint_2667 | Tint_2668 | KEGG: aav:Aave_3581 serine/threonine protein kinase; PFAM: Serine/threonine-protein kinase-like domain; SMART: serine/threonine protein kinase; Tyrosine-protein kinase, subgroup, catalytic domain. | KEGG: pol:Bpro_1338 protein serine/threonine phosphatases; PFAM: Protein phosphatase 2C-like; SMART: protein phosphatase 2C domain protein. | 0.971 |
Tint_2667 | Tint_2670 | Tint_2667 | Tint_2670 | KEGG: aav:Aave_3581 serine/threonine protein kinase; PFAM: Serine/threonine-protein kinase-like domain; SMART: serine/threonine protein kinase; Tyrosine-protein kinase, subgroup, catalytic domain. | Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | 0.727 |
Tint_2667 | Tint_2671 | Tint_2667 | Tint_2671 | KEGG: aav:Aave_3581 serine/threonine protein kinase; PFAM: Serine/threonine-protein kinase-like domain; SMART: serine/threonine protein kinase; Tyrosine-protein kinase, subgroup, catalytic domain. | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.695 |
Tint_2667 | rph | Tint_2667 | Tint_2669 | KEGG: aav:Aave_3581 serine/threonine protein kinase; PFAM: Serine/threonine-protein kinase-like domain; SMART: serine/threonine protein kinase; Tyrosine-protein kinase, subgroup, catalytic domain. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.720 |
Tint_2668 | Tint_2667 | Tint_2668 | Tint_2667 | KEGG: pol:Bpro_1338 protein serine/threonine phosphatases; PFAM: Protein phosphatase 2C-like; SMART: protein phosphatase 2C domain protein. | KEGG: aav:Aave_3581 serine/threonine protein kinase; PFAM: Serine/threonine-protein kinase-like domain; SMART: serine/threonine protein kinase; Tyrosine-protein kinase, subgroup, catalytic domain. | 0.971 |
Tint_2668 | Tint_2670 | Tint_2668 | Tint_2670 | KEGG: pol:Bpro_1338 protein serine/threonine phosphatases; PFAM: Protein phosphatase 2C-like; SMART: protein phosphatase 2C domain protein. | Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | 0.731 |
Tint_2668 | Tint_2671 | Tint_2668 | Tint_2671 | KEGG: pol:Bpro_1338 protein serine/threonine phosphatases; PFAM: Protein phosphatase 2C-like; SMART: protein phosphatase 2C domain protein. | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.693 |
Tint_2668 | rph | Tint_2668 | Tint_2669 | KEGG: pol:Bpro_1338 protein serine/threonine phosphatases; PFAM: Protein phosphatase 2C-like; SMART: protein phosphatase 2C domain protein. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.720 |
Tint_2670 | Tint_2667 | Tint_2670 | Tint_2667 | Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | KEGG: aav:Aave_3581 serine/threonine protein kinase; PFAM: Serine/threonine-protein kinase-like domain; SMART: serine/threonine protein kinase; Tyrosine-protein kinase, subgroup, catalytic domain. | 0.727 |
Tint_2670 | Tint_2668 | Tint_2670 | Tint_2668 | Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | KEGG: pol:Bpro_1338 protein serine/threonine phosphatases; PFAM: Protein phosphatase 2C-like; SMART: protein phosphatase 2C domain protein. | 0.731 |
Tint_2670 | Tint_2671 | Tint_2670 | Tint_2671 | Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.780 |
Tint_2670 | rph | Tint_2670 | Tint_2669 | Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.990 |
Tint_2671 | Tint_2667 | Tint_2671 | Tint_2667 | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | KEGG: aav:Aave_3581 serine/threonine protein kinase; PFAM: Serine/threonine-protein kinase-like domain; SMART: serine/threonine protein kinase; Tyrosine-protein kinase, subgroup, catalytic domain. | 0.695 |
Tint_2671 | Tint_2668 | Tint_2671 | Tint_2668 | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | KEGG: pol:Bpro_1338 protein serine/threonine phosphatases; PFAM: Protein phosphatase 2C-like; SMART: protein phosphatase 2C domain protein. | 0.693 |
Tint_2671 | Tint_2670 | Tint_2671 | Tint_2670 | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | 0.780 |
Tint_2671 | rph | Tint_2671 | Tint_2669 | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.810 |
rph | Tint_2667 | Tint_2669 | Tint_2667 | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | KEGG: aav:Aave_3581 serine/threonine protein kinase; PFAM: Serine/threonine-protein kinase-like domain; SMART: serine/threonine protein kinase; Tyrosine-protein kinase, subgroup, catalytic domain. | 0.720 |
rph | Tint_2668 | Tint_2669 | Tint_2668 | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | KEGG: pol:Bpro_1338 protein serine/threonine phosphatases; PFAM: Protein phosphatase 2C-like; SMART: protein phosphatase 2C domain protein. | 0.720 |
rph | Tint_2670 | Tint_2669 | Tint_2670 | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | 0.990 |
rph | Tint_2671 | Tint_2669 | Tint_2671 | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.810 |