node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ95185.1 | CAZ95186.1 | ZOBELLIA_1127 | ZOBELLIA_1128 | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator. Localized in the cytoplasm; Specificity unclear. | 0.948 |
CAZ95185.1 | CAZ95187.1 | ZOBELLIA_1127 | ZOBELLIA_1130 | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | Hypothetical protein. Putatively localized in the cytoplasm. | 0.418 |
CAZ95185.1 | CAZ97804.1 | ZOBELLIA_1127 | ZOBELLIA_3666 | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator. Localized in the cytoplasm; Specificity unclear. | 0.769 |
CAZ95185.1 | CAZ98162.1 | ZOBELLIA_1127 | ZOBELLIA_4026 | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator; Localized in the cytoplasm; Family membership. | 0.779 |
CAZ95185.1 | mutA | ZOBELLIA_1127 | ZOBELLIA_1125 | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutA codes the small subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | 0.405 |
CAZ95185.1 | mutB | ZOBELLIA_1127 | ZOBELLIA_1126 | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutB codes the large subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | 0.417 |
CAZ95186.1 | CAZ95185.1 | ZOBELLIA_1128 | ZOBELLIA_1127 | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator. Localized in the cytoplasm; Specificity unclear. | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | 0.948 |
CAZ95186.1 | CAZ95187.1 | ZOBELLIA_1128 | ZOBELLIA_1130 | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator. Localized in the cytoplasm; Specificity unclear. | Hypothetical protein. Putatively localized in the cytoplasm. | 0.418 |
CAZ95186.1 | mutA | ZOBELLIA_1128 | ZOBELLIA_1125 | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator. Localized in the cytoplasm; Specificity unclear. | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutA codes the small subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | 0.405 |
CAZ95186.1 | mutB | ZOBELLIA_1128 | ZOBELLIA_1126 | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator. Localized in the cytoplasm; Specificity unclear. | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutB codes the large subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | 0.417 |
CAZ95187.1 | CAZ95185.1 | ZOBELLIA_1130 | ZOBELLIA_1127 | Hypothetical protein. Putatively localized in the cytoplasm. | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | 0.418 |
CAZ95187.1 | CAZ95186.1 | ZOBELLIA_1130 | ZOBELLIA_1128 | Hypothetical protein. Putatively localized in the cytoplasm. | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator. Localized in the cytoplasm; Specificity unclear. | 0.418 |
CAZ97804.1 | CAZ95185.1 | ZOBELLIA_3666 | ZOBELLIA_1127 | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator. Localized in the cytoplasm; Specificity unclear. | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | 0.769 |
CAZ98162.1 | CAZ95185.1 | ZOBELLIA_4026 | ZOBELLIA_1127 | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator; Localized in the cytoplasm; Family membership. | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | 0.779 |
mutA | CAZ95185.1 | ZOBELLIA_1125 | ZOBELLIA_1127 | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutA codes the small subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | 0.405 |
mutA | CAZ95186.1 | ZOBELLIA_1125 | ZOBELLIA_1128 | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutA codes the small subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator. Localized in the cytoplasm; Specificity unclear. | 0.405 |
mutA | mutB | ZOBELLIA_1125 | ZOBELLIA_1126 | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutA codes the small subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutB codes the large subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | 0.998 |
mutB | CAZ95185.1 | ZOBELLIA_1126 | ZOBELLIA_1127 | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutB codes the large subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain. Features also in the N-terminal region a transmembrane helix, a domain of unknown function followed by another transmembrane helix. The histine kinase domain is the C-terminal region. Localized in the cytoplasmic membrane; Specificity unclear. | 0.417 |
mutB | CAZ95186.1 | ZOBELLIA_1126 | ZOBELLIA_1128 | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutB codes the large subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator. Localized in the cytoplasm; Specificity unclear. | 0.417 |
mutB | mutA | ZOBELLIA_1126 | ZOBELLIA_1125 | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutB codes the large subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | Methylmalonyl-CoA mutase is a heterodimer of a small (alpha) and a large (beta) chain. These two subunits are non-identical, yet structurally related chains. MutA codes the small subunit. Methylmalonyl-CoA mutase is an adenosylcobalamin (vitamin B12) dependent enzyme that catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Localized in the cytoplasm; High confidence in function and specificity. | 0.998 |