| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Lbys_2809 | Lbys_2810 | Lbys_2809 | Lbys_2810 | COGs: COG0861 Membrane protein TerC possibly involved in tellurium resistance; InterPro IPR005496; KEGG: cpi:Cpin_1725 integral membrane protein TerC; PFAM: Integral membrane protein TerC; SPTR: Integral membrane protein TerC; PFAM: Integral membrane protein TerC family. | COGs: COG0204 1-acyl-sn-glycerol-3-phosphate acyltransferase; InterPro IPR002123; KEGG: sli:Slin_5448 phospholipid/glycerol acyltransferase; PFAM: phospholipid/glycerol acyltransferase; SMART: phospholipid/glycerol acyltransferase; SPTR: Phospholipid/glycerol acyltransferase; PFAM: Acyltransferase; TIGRFAM: 1-acyl-sn-glycerol-3-phosphate acyltransferases. | 0.774 |
| Lbys_2809 | gatC | Lbys_2809 | Lbys_2811 | COGs: COG0861 Membrane protein TerC possibly involved in tellurium resistance; InterPro IPR005496; KEGG: cpi:Cpin_1725 integral membrane protein TerC; PFAM: Integral membrane protein TerC; SPTR: Integral membrane protein TerC; PFAM: Integral membrane protein TerC family. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.776 |
| Lbys_2810 | Lbys_2809 | Lbys_2810 | Lbys_2809 | COGs: COG0204 1-acyl-sn-glycerol-3-phosphate acyltransferase; InterPro IPR002123; KEGG: sli:Slin_5448 phospholipid/glycerol acyltransferase; PFAM: phospholipid/glycerol acyltransferase; SMART: phospholipid/glycerol acyltransferase; SPTR: Phospholipid/glycerol acyltransferase; PFAM: Acyltransferase; TIGRFAM: 1-acyl-sn-glycerol-3-phosphate acyltransferases. | COGs: COG0861 Membrane protein TerC possibly involved in tellurium resistance; InterPro IPR005496; KEGG: cpi:Cpin_1725 integral membrane protein TerC; PFAM: Integral membrane protein TerC; SPTR: Integral membrane protein TerC; PFAM: Integral membrane protein TerC family. | 0.774 |
| Lbys_2810 | gatC | Lbys_2810 | Lbys_2811 | COGs: COG0204 1-acyl-sn-glycerol-3-phosphate acyltransferase; InterPro IPR002123; KEGG: sli:Slin_5448 phospholipid/glycerol acyltransferase; PFAM: phospholipid/glycerol acyltransferase; SMART: phospholipid/glycerol acyltransferase; SPTR: Phospholipid/glycerol acyltransferase; PFAM: Acyltransferase; TIGRFAM: 1-acyl-sn-glycerol-3-phosphate acyltransferases. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.812 |
| asnS | aspS | Lbys_3177 | Lbys_3169 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR006195:IPR010916:IPR002312:IPR004365:IPR 004364:IPR004522; KEGG: dfe:Dfer_4215 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.410 |
| asnS | gatA | Lbys_3177 | Lbys_1579 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR006195:IPR010916:IPR002312:IPR004365:IPR 004364:IPR004522; KEGG: dfe:Dfer_4215 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.989 |
| asnS | gatB | Lbys_3177 | Lbys_1720 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR006195:IPR010916:IPR002312:IPR004365:IPR 004364:IPR004522; KEGG: dfe:Dfer_4215 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.998 |
| asnS | gatC | Lbys_3177 | Lbys_2811 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR006195:IPR010916:IPR002312:IPR004365:IPR 004364:IPR004522; KEGG: dfe:Dfer_4215 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.968 |
| asnS | glnS | Lbys_3177 | Lbys_1650 | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR006195:IPR010916:IPR002312:IPR004365:IPR 004364:IPR004522; KEGG: dfe:Dfer_4215 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058:IPR020059:IPR020060:IPR001412:IPR 004514; KEGG: dfe:Dfer_2503 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; TIGRFAM: glutaminyl-tRNA synthetase. | 0.746 |
| aspS | asnS | Lbys_3169 | Lbys_3177 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR006195:IPR010916:IPR002312:IPR004365:IPR 004364:IPR004522; KEGG: dfe:Dfer_4215 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | 0.410 |
| aspS | gatA | Lbys_3169 | Lbys_1579 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.819 |
| aspS | gatB | Lbys_3169 | Lbys_1720 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.997 |
| aspS | gatC | Lbys_3169 | Lbys_2811 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.939 |
| aspS | glnS | Lbys_3169 | Lbys_1650 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020058:IPR020059:IPR020060:IPR001412:IPR 004514; KEGG: dfe:Dfer_2503 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; SPTR: Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; TIGRFAM: glutaminyl-tRNA synthetase. | 0.484 |
| atpH | gatB | Lbys_3609 | Lbys_1720 | ATP synthase F1 subcomplex delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.701 |
| atpH | gatC | Lbys_3609 | Lbys_2811 | ATP synthase F1 subcomplex delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.795 |
| atpH | rplJ | Lbys_3609 | Lbys_2613 | ATP synthase F1 subcomplex delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | LSU ribosomal protein L10P; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family. | 0.864 |
| atpH | rpsN | Lbys_3609 | Lbys_1817 | ATP synthase F1 subcomplex delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | SSU ribosomal protein S14P; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family. | 0.844 |
| gatA | asnS | Lbys_1579 | Lbys_3177 | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR006195:IPR010916:IPR002312:IPR004365:IPR 004364:IPR004522; KEGG: dfe:Dfer_4215 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. | 0.989 |
| gatA | aspS | Lbys_1579 | Lbys_3169 | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.819 |