node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AFK06504.1 | AFK06505.1 | Theba_0790 | Theba_0791 | Putative permease; PFAM: Domain of unknown function DUF20. | L-asparaginase/GlutRNAGln amidotransferase subunit D; PFAM: Asparaginase; TIGRFAM: L-asparaginases, type II. | 0.801 |
AFK06504.1 | AFK06506.1 | Theba_0790 | Theba_0792 | Putative permease; PFAM: Domain of unknown function DUF20. | Putative Fe-S oxidoreductase; PFAM: Radical SAM superfamily. | 0.801 |
AFK06504.1 | clpX | Theba_0790 | Theba_0793 | Putative permease; PFAM: Domain of unknown function DUF20. | Endopeptidase Clp ATP-binding regulatory subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.576 |
AFK06504.1 | tsaD | Theba_0790 | Theba_0794 | Putative permease; PFAM: Domain of unknown function DUF20. | Putative glycoprotease GCP; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction; Belongs to the KAE1 / TsaD family. | 0.579 |
AFK06505.1 | AFK06504.1 | Theba_0791 | Theba_0790 | L-asparaginase/GlutRNAGln amidotransferase subunit D; PFAM: Asparaginase; TIGRFAM: L-asparaginases, type II. | Putative permease; PFAM: Domain of unknown function DUF20. | 0.801 |
AFK06505.1 | AFK06506.1 | Theba_0791 | Theba_0792 | L-asparaginase/GlutRNAGln amidotransferase subunit D; PFAM: Asparaginase; TIGRFAM: L-asparaginases, type II. | Putative Fe-S oxidoreductase; PFAM: Radical SAM superfamily. | 0.788 |
AFK06505.1 | clpX | Theba_0791 | Theba_0793 | L-asparaginase/GlutRNAGln amidotransferase subunit D; PFAM: Asparaginase; TIGRFAM: L-asparaginases, type II. | Endopeptidase Clp ATP-binding regulatory subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.568 |
AFK06505.1 | tsaD | Theba_0791 | Theba_0794 | L-asparaginase/GlutRNAGln amidotransferase subunit D; PFAM: Asparaginase; TIGRFAM: L-asparaginases, type II. | Putative glycoprotease GCP; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction; Belongs to the KAE1 / TsaD family. | 0.592 |
AFK06506.1 | AFK06504.1 | Theba_0792 | Theba_0790 | Putative Fe-S oxidoreductase; PFAM: Radical SAM superfamily. | Putative permease; PFAM: Domain of unknown function DUF20. | 0.801 |
AFK06506.1 | AFK06505.1 | Theba_0792 | Theba_0791 | Putative Fe-S oxidoreductase; PFAM: Radical SAM superfamily. | L-asparaginase/GlutRNAGln amidotransferase subunit D; PFAM: Asparaginase; TIGRFAM: L-asparaginases, type II. | 0.788 |
AFK06506.1 | clpX | Theba_0792 | Theba_0793 | Putative Fe-S oxidoreductase; PFAM: Radical SAM superfamily. | Endopeptidase Clp ATP-binding regulatory subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.578 |
AFK06506.1 | tsaD | Theba_0792 | Theba_0794 | Putative Fe-S oxidoreductase; PFAM: Radical SAM superfamily. | Putative glycoprotease GCP; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction; Belongs to the KAE1 / TsaD family. | 0.578 |
atpD | clpX | Theba_1048 | Theba_0793 | ATP synthase, F1 beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Endopeptidase Clp ATP-binding regulatory subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.773 |
atpD | ftsH | Theba_1048 | Theba_0376 | ATP synthase, F1 beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | ATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.551 |
atpD | groL | Theba_1048 | Theba_2219 | ATP synthase, F1 beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.588 |
clpP | clpX | Theba_0891 | Theba_0793 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Endopeptidase Clp ATP-binding regulatory subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.989 |
clpP | ftsH | Theba_0891 | Theba_0376 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.444 |
clpP | groL | Theba_0891 | Theba_2219 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.739 |
clpP | hfq | Theba_0891 | Theba_0821 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | RNA chaperone Hfq; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Belongs to the Hfq family. | 0.461 |
clpP | lon | Theba_0891 | Theba_0764 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.657 |