| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ97855.1 | CAZ97856.1 | ZOBELLIA_3717 | ZOBELLIA_3718 | Sodium/solute symporter; Sodium/substrate symport is a widespread mechanism of solute transport across cytoplasmic membranes of cells. Thereby the energy stored in an inwardly directed electrochemical sodium gradient (sodium motive force, SMF) is used to drive solute accumulation against a concentration gradient; Contains thirteen transmembrane helices; Localized in the cytoplasmic membrane; Family membership; Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family. | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.951 |
| CAZ97855.1 | CAZ97974.1 | ZOBELLIA_3717 | ZOBELLIA_3836 | Sodium/solute symporter; Sodium/substrate symport is a widespread mechanism of solute transport across cytoplasmic membranes of cells. Thereby the energy stored in an inwardly directed electrochemical sodium gradient (sodium motive force, SMF) is used to drive solute accumulation against a concentration gradient; Contains thirteen transmembrane helices; Localized in the cytoplasmic membrane; Family membership; Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family. | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | 0.757 |
| CAZ97856.1 | CAZ97855.1 | ZOBELLIA_3718 | ZOBELLIA_3717 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Sodium/solute symporter; Sodium/substrate symport is a widespread mechanism of solute transport across cytoplasmic membranes of cells. Thereby the energy stored in an inwardly directed electrochemical sodium gradient (sodium motive force, SMF) is used to drive solute accumulation against a concentration gradient; Contains thirteen transmembrane helices; Localized in the cytoplasmic membrane; Family membership; Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family. | 0.951 |
| CAZ97856.1 | CAZ97974.1 | ZOBELLIA_3718 | ZOBELLIA_3836 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | 0.654 |
| CAZ97974.1 | CAZ97855.1 | ZOBELLIA_3836 | ZOBELLIA_3717 | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | Sodium/solute symporter; Sodium/substrate symport is a widespread mechanism of solute transport across cytoplasmic membranes of cells. Thereby the energy stored in an inwardly directed electrochemical sodium gradient (sodium motive force, SMF) is used to drive solute accumulation against a concentration gradient; Contains thirteen transmembrane helices; Localized in the cytoplasmic membrane; Family membership; Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family. | 0.757 |
| CAZ97974.1 | CAZ97856.1 | ZOBELLIA_3836 | ZOBELLIA_3718 | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.654 |
| CAZ97974.1 | CAZ97975.1 | ZOBELLIA_3836 | ZOBELLIA_3837 | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | Conserved protein belonging to the DUF893 family; Contains nine transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.433 |
| CAZ97974.1 | CAZ97976.1 | ZOBELLIA_3836 | ZOBELLIA_3838 | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | Putative protein. | 0.570 |
| CAZ97974.1 | dnaQ | ZOBELLIA_3836 | ZOBELLIA_3835 | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | The epsilon subunit of DNA polymerase III is responsible of the proofreading 3'-5' exonuclease activity; The DNA polymerase III or replicase is responsible for most of the replicative synthesis in bacteria. It exhibits a DNA polymerase activity (alpha chain) and a 3' to 5' exonuclease proofreading activity; Localized in the cytoplasm; High confidence in function and specificity. | 0.952 |
| CAZ97974.1 | guaA | ZOBELLIA_3836 | ZOBELLIA_568 | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP. | 0.411 |
| CAZ97975.1 | CAZ97974.1 | ZOBELLIA_3837 | ZOBELLIA_3836 | Conserved protein belonging to the DUF893 family; Contains nine transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | 0.433 |
| CAZ97975.1 | CAZ97976.1 | ZOBELLIA_3837 | ZOBELLIA_3838 | Conserved protein belonging to the DUF893 family; Contains nine transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Putative protein. | 0.572 |
| CAZ97975.1 | dnaQ | ZOBELLIA_3837 | ZOBELLIA_3835 | Conserved protein belonging to the DUF893 family; Contains nine transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | The epsilon subunit of DNA polymerase III is responsible of the proofreading 3'-5' exonuclease activity; The DNA polymerase III or replicase is responsible for most of the replicative synthesis in bacteria. It exhibits a DNA polymerase activity (alpha chain) and a 3' to 5' exonuclease proofreading activity; Localized in the cytoplasm; High confidence in function and specificity. | 0.462 |
| CAZ97976.1 | CAZ97974.1 | ZOBELLIA_3838 | ZOBELLIA_3836 | Putative protein. | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | 0.570 |
| CAZ97976.1 | CAZ97975.1 | ZOBELLIA_3838 | ZOBELLIA_3837 | Putative protein. | Conserved protein belonging to the DUF893 family; Contains nine transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.572 |
| CAZ97976.1 | dnaQ | ZOBELLIA_3838 | ZOBELLIA_3835 | Putative protein. | The epsilon subunit of DNA polymerase III is responsible of the proofreading 3'-5' exonuclease activity; The DNA polymerase III or replicase is responsible for most of the replicative synthesis in bacteria. It exhibits a DNA polymerase activity (alpha chain) and a 3' to 5' exonuclease proofreading activity; Localized in the cytoplasm; High confidence in function and specificity. | 0.570 |
| dnaQ | CAZ97974.1 | ZOBELLIA_3835 | ZOBELLIA_3836 | The epsilon subunit of DNA polymerase III is responsible of the proofreading 3'-5' exonuclease activity; The DNA polymerase III or replicase is responsible for most of the replicative synthesis in bacteria. It exhibits a DNA polymerase activity (alpha chain) and a 3' to 5' exonuclease proofreading activity; Localized in the cytoplasm; High confidence in function and specificity. | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | 0.952 |
| dnaQ | CAZ97975.1 | ZOBELLIA_3835 | ZOBELLIA_3837 | The epsilon subunit of DNA polymerase III is responsible of the proofreading 3'-5' exonuclease activity; The DNA polymerase III or replicase is responsible for most of the replicative synthesis in bacteria. It exhibits a DNA polymerase activity (alpha chain) and a 3' to 5' exonuclease proofreading activity; Localized in the cytoplasm; High confidence in function and specificity. | Conserved protein belonging to the DUF893 family; Contains nine transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.462 |
| dnaQ | CAZ97976.1 | ZOBELLIA_3835 | ZOBELLIA_3838 | The epsilon subunit of DNA polymerase III is responsible of the proofreading 3'-5' exonuclease activity; The DNA polymerase III or replicase is responsible for most of the replicative synthesis in bacteria. It exhibits a DNA polymerase activity (alpha chain) and a 3' to 5' exonuclease proofreading activity; Localized in the cytoplasm; High confidence in function and specificity. | Putative protein. | 0.570 |
| guaA | CAZ97974.1 | ZOBELLIA_568 | ZOBELLIA_3836 | GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP. | Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...] | 0.411 |