| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MCA2011 | MCA2012 | MCA2011 | MCA2012 | Identified by similarity to SP:Q8Z9E1; match to protein family HMM PF07731; match to protein family HMM PF07732; match to protein family HMM TIGR01409. | Hypothetical protein; Identified by Glimmer2; putative. | 0.525 |
| MCA2012 | MCA2011 | MCA2012 | MCA2011 | Hypothetical protein; Identified by Glimmer2; putative. | Identified by similarity to SP:Q8Z9E1; match to protein family HMM PF07731; match to protein family HMM PF07732; match to protein family HMM TIGR01409. | 0.525 |
| MCA2012 | MCA2016 | MCA2012 | MCA2016 | Hypothetical protein; Identified by Glimmer2; putative. | Conserved hypothetical protein; Identified by similarity to GP:17427467; match to protein family HMM PF06155. | 0.423 |
| MCA2012 | hslU | MCA2012 | MCA2015 | Hypothetical protein; Identified by Glimmer2; putative. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.423 |
| MCA2012 | hslV | MCA2012 | MCA2014 | Hypothetical protein; Identified by Glimmer2; putative. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.423 |
| MCA2012 | proS | MCA2012 | MCA2013 | Hypothetical protein; Identified by Glimmer2; putative. | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.532 |
| MCA2016 | MCA2012 | MCA2016 | MCA2012 | Conserved hypothetical protein; Identified by similarity to GP:17427467; match to protein family HMM PF06155. | Hypothetical protein; Identified by Glimmer2; putative. | 0.423 |
| MCA2016 | hslU | MCA2016 | MCA2015 | Conserved hypothetical protein; Identified by similarity to GP:17427467; match to protein family HMM PF06155. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.842 |
| MCA2016 | hslV | MCA2016 | MCA2014 | Conserved hypothetical protein; Identified by similarity to GP:17427467; match to protein family HMM PF06155. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.849 |
| MCA2016 | proS | MCA2016 | MCA2013 | Conserved hypothetical protein; Identified by similarity to GP:17427467; match to protein family HMM PF06155. | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.598 |
| hslU | MCA2012 | MCA2015 | MCA2012 | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Hypothetical protein; Identified by Glimmer2; putative. | 0.423 |
| hslU | MCA2016 | MCA2015 | MCA2016 | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Conserved hypothetical protein; Identified by similarity to GP:17427467; match to protein family HMM PF06155. | 0.842 |
| hslU | hslV | MCA2015 | MCA2014 | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
| hslU | proS | MCA2015 | MCA2013 | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.640 |
| hslV | MCA2012 | MCA2014 | MCA2012 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Hypothetical protein; Identified by Glimmer2; putative. | 0.423 |
| hslV | MCA2016 | MCA2014 | MCA2016 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Conserved hypothetical protein; Identified by similarity to GP:17427467; match to protein family HMM PF06155. | 0.849 |
| hslV | hslU | MCA2014 | MCA2015 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.999 |
| hslV | proS | MCA2014 | MCA2013 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.620 |
| proS | MCA2012 | MCA2013 | MCA2012 | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | Hypothetical protein; Identified by Glimmer2; putative. | 0.532 |
| proS | MCA2016 | MCA2013 | MCA2016 | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | Conserved hypothetical protein; Identified by similarity to GP:17427467; match to protein family HMM PF06155. | 0.598 |