node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
FSU_0657 | argJ | FSU_0657 | FSU_0655 | Conserved hypothetical protein; Identified by match to protein family HMM PF06144; match to protein family HMM TIGR01128. | Glutamate N-acetyltransferase/amino-acid acetyltransferase; Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Belongs to the ArgJ family. | 0.579 |
FSU_0657 | greA | FSU_0657 | FSU_0656 | Conserved hypothetical protein; Identified by match to protein family HMM PF06144; match to protein family HMM TIGR01128. | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | 0.784 |
FSU_0703 | ftsH | FSU_0703 | FSU_0030 | Type II secretion system protein; Identified by match to protein family HMM PF00437. | Cell division protein 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. | 0.611 |
FSU_0703 | greA | FSU_0703 | FSU_0656 | Type II secretion system protein; Identified by match to protein family HMM PF00437. | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | 0.608 |
FSU_0703 | rub_1 | FSU_0703 | FSU_1835 | Type II secretion system protein; Identified by match to protein family HMM PF00437. | Rubredoxin; Identified by similarity to SP:P00269; match to protein family HMM PF00301. | 0.608 |
FSU_0703 | rub_2 | FSU_0703 | FSU_2620 | Type II secretion system protein; Identified by match to protein family HMM PF00437. | Rubredoxin; Identified by similarity to SP:P00269; match to protein family HMM PF00301. | 0.608 |
argJ | FSU_0657 | FSU_0655 | FSU_0657 | Glutamate N-acetyltransferase/amino-acid acetyltransferase; Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Belongs to the ArgJ family. | Conserved hypothetical protein; Identified by match to protein family HMM PF06144; match to protein family HMM TIGR01128. | 0.579 |
argJ | greA | FSU_0655 | FSU_0656 | Glutamate N-acetyltransferase/amino-acid acetyltransferase; Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Belongs to the ArgJ family. | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | 0.553 |
ftsH | FSU_0703 | FSU_0030 | FSU_0703 | Cell division protein 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. | Type II secretion system protein; Identified by match to protein family HMM PF00437. | 0.611 |
ftsH | greA | FSU_0030 | FSU_0656 | Cell division protein 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. | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | 0.715 |
ftsH | groEL | FSU_0030 | FSU_0456 | Cell division protein 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. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.772 |
ftsH | rub_1 | FSU_0030 | FSU_1835 | Cell division protein 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. | Rubredoxin; Identified by similarity to SP:P00269; match to protein family HMM PF00301. | 0.638 |
ftsH | rub_2 | FSU_0030 | FSU_2620 | Cell division protein 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. | Rubredoxin; Identified by similarity to SP:P00269; match to protein family HMM PF00301. | 0.638 |
greA | FSU_0657 | FSU_0656 | FSU_0657 | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | Conserved hypothetical protein; Identified by match to protein family HMM PF06144; match to protein family HMM TIGR01128. | 0.784 |
greA | FSU_0703 | FSU_0656 | FSU_0703 | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | Type II secretion system protein; Identified by match to protein family HMM PF00437. | 0.608 |
greA | argJ | FSU_0656 | FSU_0655 | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | Glutamate N-acetyltransferase/amino-acid acetyltransferase; Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Belongs to the ArgJ family. | 0.553 |
greA | ftsH | FSU_0656 | FSU_0030 | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | Cell division protein 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. | 0.715 |
greA | groEL | FSU_0656 | FSU_0456 | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.652 |
greA | rpoB | FSU_0656 | FSU_1734 | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | DNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.865 |
greA | rpoC_1 | FSU_0656 | FSU_1450 | Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | DNA-directed RNA polymerase, beta' subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.865 |