| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADU47841.1 | ADU47843.1 | Intca_1325 | Intca_1327 | COGs: COG1234 Metal-dependent hydrolase of the beta-lactamase superfamily III; KEGG: kse:Ksed_09930 metal-dependent hydrolase, beta-lactamase superfamily III; SPTR: Putative uncharacterized protein; PFAM: Metallo-beta-lactamase superfamily. | 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. | 0.656 |
| ADU47841.1 | ADU47844.1 | Intca_1325 | Intca_1328 | COGs: COG1234 Metal-dependent hydrolase of the beta-lactamase superfamily III; KEGG: kse:Ksed_09930 metal-dependent hydrolase, beta-lactamase superfamily III; SPTR: Putative uncharacterized protein; PFAM: Metallo-beta-lactamase superfamily. | Oxidoreductase molybdopterin binding protein; COGs: COG2041 Sulfite oxidase; InterPro IPR000572: IPR005066; KEGG: art:Arth_1443 oxidoreductase, molybdopterin binding; PFAM: oxidoreductase molybdopterin binding; Mo-co oxidoreductase dimerisation domain; SPTR: Oxidoreductase, molybdopterin binding; PFAM: Mo-co oxidoreductase dimerisation domain; Oxidoreductase molybdopterin binding domain. | 0.548 |
| ADU47841.1 | ADU48556.1 | Intca_1325 | Intca_2045 | COGs: COG1234 Metal-dependent hydrolase of the beta-lactamase superfamily III; KEGG: kse:Ksed_09930 metal-dependent hydrolase, beta-lactamase superfamily III; SPTR: Putative uncharacterized protein; PFAM: Metallo-beta-lactamase superfamily. | COGs: COG0557 Exoribonuclease R; InterPro IPR001900; KEGG: kse:Ksed_12120 exoribonuclease R; PFAM: ribonuclease II; SPTR: Putative ribonuclease R; PFAM: RNB domain. | 0.409 |
| ADU47841.1 | rph | Intca_1325 | Intca_1326 | COGs: COG1234 Metal-dependent hydrolase of the beta-lactamase superfamily III; KEGG: kse:Ksed_09930 metal-dependent hydrolase, beta-lactamase superfamily III; SPTR: Putative uncharacterized protein; PFAM: Metallo-beta-lactamase superfamily. | RNAse 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. | 0.743 |
| ADU47843.1 | ADU47841.1 | Intca_1327 | Intca_1325 | 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. | COGs: COG1234 Metal-dependent hydrolase of the beta-lactamase superfamily III; KEGG: kse:Ksed_09930 metal-dependent hydrolase, beta-lactamase superfamily III; SPTR: Putative uncharacterized protein; PFAM: Metallo-beta-lactamase superfamily. | 0.656 |
| ADU47843.1 | ADU47844.1 | Intca_1327 | Intca_1328 | 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. | Oxidoreductase molybdopterin binding protein; COGs: COG2041 Sulfite oxidase; InterPro IPR000572: IPR005066; KEGG: art:Arth_1443 oxidoreductase, molybdopterin binding; PFAM: oxidoreductase molybdopterin binding; Mo-co oxidoreductase dimerisation domain; SPTR: Oxidoreductase, molybdopterin binding; PFAM: Mo-co oxidoreductase dimerisation domain; Oxidoreductase molybdopterin binding domain. | 0.790 |
| ADU47843.1 | rph | Intca_1327 | Intca_1326 | 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. | RNAse 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. | 0.992 |
| ADU47844.1 | ADU47841.1 | Intca_1328 | Intca_1325 | Oxidoreductase molybdopterin binding protein; COGs: COG2041 Sulfite oxidase; InterPro IPR000572: IPR005066; KEGG: art:Arth_1443 oxidoreductase, molybdopterin binding; PFAM: oxidoreductase molybdopterin binding; Mo-co oxidoreductase dimerisation domain; SPTR: Oxidoreductase, molybdopterin binding; PFAM: Mo-co oxidoreductase dimerisation domain; Oxidoreductase molybdopterin binding domain. | COGs: COG1234 Metal-dependent hydrolase of the beta-lactamase superfamily III; KEGG: kse:Ksed_09930 metal-dependent hydrolase, beta-lactamase superfamily III; SPTR: Putative uncharacterized protein; PFAM: Metallo-beta-lactamase superfamily. | 0.548 |
| ADU47844.1 | ADU47843.1 | Intca_1328 | Intca_1327 | Oxidoreductase molybdopterin binding protein; COGs: COG2041 Sulfite oxidase; InterPro IPR000572: IPR005066; KEGG: art:Arth_1443 oxidoreductase, molybdopterin binding; PFAM: oxidoreductase molybdopterin binding; Mo-co oxidoreductase dimerisation domain; SPTR: Oxidoreductase, molybdopterin binding; PFAM: Mo-co oxidoreductase dimerisation domain; Oxidoreductase molybdopterin binding 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. | 0.790 |
| ADU47844.1 | rph | Intca_1328 | Intca_1326 | Oxidoreductase molybdopterin binding protein; COGs: COG2041 Sulfite oxidase; InterPro IPR000572: IPR005066; KEGG: art:Arth_1443 oxidoreductase, molybdopterin binding; PFAM: oxidoreductase molybdopterin binding; Mo-co oxidoreductase dimerisation domain; SPTR: Oxidoreductase, molybdopterin binding; PFAM: Mo-co oxidoreductase dimerisation domain; Oxidoreductase molybdopterin binding domain. | RNAse 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. | 0.790 |
| ADU48423.1 | ADU48556.1 | Intca_1912 | Intca_2045 | 3'-5' exonuclease; COGs: COG0349 Ribonuclease D; InterPro IPR002562: IPR002121: IPR018312; KEGG: sma:SAV_2231 ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain protein; SMART: 3'-5' exonuclease; HRDC domain protein; SPTR: Putative ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain; TIGRFAM: ribonuclease D. | COGs: COG0557 Exoribonuclease R; InterPro IPR001900; KEGG: kse:Ksed_12120 exoribonuclease R; PFAM: ribonuclease II; SPTR: Putative ribonuclease R; PFAM: RNB domain. | 0.932 |
| ADU48423.1 | rph | Intca_1912 | Intca_1326 | 3'-5' exonuclease; COGs: COG0349 Ribonuclease D; InterPro IPR002562: IPR002121: IPR018312; KEGG: sma:SAV_2231 ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain protein; SMART: 3'-5' exonuclease; HRDC domain protein; SPTR: Putative ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain; TIGRFAM: ribonuclease D. | RNAse 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. | 0.929 |
| ADU48423.1 | rpsD | Intca_1912 | Intca_2725 | 3'-5' exonuclease; COGs: COG0349 Ribonuclease D; InterPro IPR002562: IPR002121: IPR018312; KEGG: sma:SAV_2231 ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain protein; SMART: 3'-5' exonuclease; HRDC domain protein; SPTR: Putative ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain; TIGRFAM: ribonuclease D. | SSU ribosomal protein S4P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. | 0.868 |
| ADU48423.1 | rpsG | Intca_1912 | Intca_2761 | 3'-5' exonuclease; COGs: COG0349 Ribonuclease D; InterPro IPR002562: IPR002121: IPR018312; KEGG: sma:SAV_2231 ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain protein; SMART: 3'-5' exonuclease; HRDC domain protein; SPTR: Putative ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain; TIGRFAM: ribonuclease D. | SSU ribosomal protein S7P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family. | 0.762 |
| ADU48423.1 | rpsK | Intca_1912 | Intca_2726 | 3'-5' exonuclease; COGs: COG0349 Ribonuclease D; InterPro IPR002562: IPR002121: IPR018312; KEGG: sma:SAV_2231 ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain protein; SMART: 3'-5' exonuclease; HRDC domain protein; SPTR: Putative ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain; TIGRFAM: ribonuclease D. | SSU ribosomal protein S11P; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family. | 0.855 |
| ADU48423.1 | rpsL | Intca_1912 | Intca_2762 | 3'-5' exonuclease; COGs: COG0349 Ribonuclease D; InterPro IPR002562: IPR002121: IPR018312; KEGG: sma:SAV_2231 ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain protein; SMART: 3'-5' exonuclease; HRDC domain protein; SPTR: Putative ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain; TIGRFAM: ribonuclease D. | SSU ribosomal protein S12P; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. | 0.757 |
| ADU48423.1 | rpsO | Intca_1912 | Intca_2197 | 3'-5' exonuclease; COGs: COG0349 Ribonuclease D; InterPro IPR002562: IPR002121: IPR018312; KEGG: sma:SAV_2231 ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain protein; SMART: 3'-5' exonuclease; HRDC domain protein; SPTR: Putative ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain; TIGRFAM: ribonuclease D. | SSU ribosomal protein S15P; Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. | 0.752 |
| ADU48556.1 | ADU47841.1 | Intca_2045 | Intca_1325 | COGs: COG0557 Exoribonuclease R; InterPro IPR001900; KEGG: kse:Ksed_12120 exoribonuclease R; PFAM: ribonuclease II; SPTR: Putative ribonuclease R; PFAM: RNB domain. | COGs: COG1234 Metal-dependent hydrolase of the beta-lactamase superfamily III; KEGG: kse:Ksed_09930 metal-dependent hydrolase, beta-lactamase superfamily III; SPTR: Putative uncharacterized protein; PFAM: Metallo-beta-lactamase superfamily. | 0.409 |
| ADU48556.1 | ADU48423.1 | Intca_2045 | Intca_1912 | COGs: COG0557 Exoribonuclease R; InterPro IPR001900; KEGG: kse:Ksed_12120 exoribonuclease R; PFAM: ribonuclease II; SPTR: Putative ribonuclease R; PFAM: RNB domain. | 3'-5' exonuclease; COGs: COG0349 Ribonuclease D; InterPro IPR002562: IPR002121: IPR018312; KEGG: sma:SAV_2231 ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain protein; SMART: 3'-5' exonuclease; HRDC domain protein; SPTR: Putative ribonuclease D; PFAM: 3'-5' exonuclease; HRDC domain; TIGRFAM: ribonuclease D. | 0.932 |
| ADU48556.1 | rph | Intca_2045 | Intca_1326 | COGs: COG0557 Exoribonuclease R; InterPro IPR001900; KEGG: kse:Ksed_12120 exoribonuclease R; PFAM: ribonuclease II; SPTR: Putative ribonuclease R; PFAM: RNB domain. | RNAse 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. | 0.932 |