node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Mettu_0421 | Mettu_0730 | Mettu_0421 | Mettu_0730 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | KEGG- svo-SVI_3119 serine/threonine protein kinase; PFAM- Serine/threonine-protein kinase-like domain; Leucine-rich repeat; SMART- Serine/threonine-protein kinase domain; Tyrosine-protein kinase, subgroup, catalytic domain; Leucine-rich repeat, typical subtype | 0.940 |
Mettu_0421 | Mettu_1336 | Mettu_0421 | Mettu_1336 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | 0.757 |
Mettu_0421 | Mettu_2595 | Mettu_0421 | Mettu_2595 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | 0.757 |
Mettu_0421 | Mettu_4189 | Mettu_0421 | Mettu_4189 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | TIGRFAM- RNA helicase, ATP-dependent DEAH box, HrpA type; PFAM- Helicase-associated region; DNA/RNA helicase, C-terminal; Domain of unknown function DUF1605; KEGG- mca-MCA1482 ATP-dependent helicase HrpA; SMART- DEAD-like helicase, N-terminal; ATPase, AAA+ type, core; DNA/RNA helicase, C-terminal | 0.773 |
Mettu_0730 | Mettu_0421 | Mettu_0730 | Mettu_0421 | KEGG- svo-SVI_3119 serine/threonine protein kinase; PFAM- Serine/threonine-protein kinase-like domain; Leucine-rich repeat; SMART- Serine/threonine-protein kinase domain; Tyrosine-protein kinase, subgroup, catalytic domain; Leucine-rich repeat, typical subtype | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | 0.940 |
Mettu_0730 | Mettu_1336 | Mettu_0730 | Mettu_1336 | KEGG- svo-SVI_3119 serine/threonine protein kinase; PFAM- Serine/threonine-protein kinase-like domain; Leucine-rich repeat; SMART- Serine/threonine-protein kinase domain; Tyrosine-protein kinase, subgroup, catalytic domain; Leucine-rich repeat, typical subtype | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | 0.897 |
Mettu_0730 | Mettu_2595 | Mettu_0730 | Mettu_2595 | KEGG- svo-SVI_3119 serine/threonine protein kinase; PFAM- Serine/threonine-protein kinase-like domain; Leucine-rich repeat; SMART- Serine/threonine-protein kinase domain; Tyrosine-protein kinase, subgroup, catalytic domain; Leucine-rich repeat, typical subtype | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | 0.897 |
Mettu_0730 | Mettu_4189 | Mettu_0730 | Mettu_4189 | KEGG- svo-SVI_3119 serine/threonine protein kinase; PFAM- Serine/threonine-protein kinase-like domain; Leucine-rich repeat; SMART- Serine/threonine-protein kinase domain; Tyrosine-protein kinase, subgroup, catalytic domain; Leucine-rich repeat, typical subtype | TIGRFAM- RNA helicase, ATP-dependent DEAH box, HrpA type; PFAM- Helicase-associated region; DNA/RNA helicase, C-terminal; Domain of unknown function DUF1605; KEGG- mca-MCA1482 ATP-dependent helicase HrpA; SMART- DEAD-like helicase, N-terminal; ATPase, AAA+ type, core; DNA/RNA helicase, C-terminal | 0.937 |
Mettu_1336 | Mettu_0421 | Mettu_1336 | Mettu_0421 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | 0.757 |
Mettu_1336 | Mettu_0730 | Mettu_1336 | Mettu_0730 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | KEGG- svo-SVI_3119 serine/threonine protein kinase; PFAM- Serine/threonine-protein kinase-like domain; Leucine-rich repeat; SMART- Serine/threonine-protein kinase domain; Tyrosine-protein kinase, subgroup, catalytic domain; Leucine-rich repeat, typical subtype | 0.897 |
Mettu_1336 | Mettu_2829 | Mettu_1336 | Mettu_2829 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | 30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence | 0.887 |
Mettu_1336 | Mettu_4189 | Mettu_1336 | Mettu_4189 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | TIGRFAM- RNA helicase, ATP-dependent DEAH box, HrpA type; PFAM- Helicase-associated region; DNA/RNA helicase, C-terminal; Domain of unknown function DUF1605; KEGG- mca-MCA1482 ATP-dependent helicase HrpA; SMART- DEAD-like helicase, N-terminal; ATPase, AAA+ type, core; DNA/RNA helicase, C-terminal | 0.741 |
Mettu_1336 | pyrG | Mettu_1336 | Mettu_2728 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates | 0.805 |
Mettu_1336 | rpsD | Mettu_1336 | Mettu_1309 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | 30S ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit | 0.999 |
Mettu_2595 | Mettu_0421 | Mettu_2595 | Mettu_0421 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | 0.757 |
Mettu_2595 | Mettu_0730 | Mettu_2595 | Mettu_0730 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | KEGG- svo-SVI_3119 serine/threonine protein kinase; PFAM- Serine/threonine-protein kinase-like domain; Leucine-rich repeat; SMART- Serine/threonine-protein kinase domain; Tyrosine-protein kinase, subgroup, catalytic domain; Leucine-rich repeat, typical subtype | 0.897 |
Mettu_2595 | Mettu_2829 | Mettu_2595 | Mettu_2829 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | 30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence | 0.810 |
Mettu_2595 | Mettu_4189 | Mettu_2595 | Mettu_4189 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | TIGRFAM- RNA helicase, ATP-dependent DEAH box, HrpA type; PFAM- Helicase-associated region; DNA/RNA helicase, C-terminal; Domain of unknown function DUF1605; KEGG- mca-MCA1482 ATP-dependent helicase HrpA; SMART- DEAD-like helicase, N-terminal; ATPase, AAA+ type, core; DNA/RNA helicase, C-terminal | 0.741 |
Mettu_2595 | pyrG | Mettu_2595 | Mettu_2728 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates | 0.600 |
Mettu_2595 | rpsD | Mettu_2595 | Mettu_1309 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | 30S ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit | 0.970 |