| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ95123.1 | cspA1 | ZOBELLIA_1066 | ZOBELLIA_1065 | DEAD/DEAH RNA helicase; Protein that could be involved in ATP-dependent RNA unwinding in a variety of cellular processes, including ribosome assembly, protein synthesis, and RNA degradation; Contains a DEAD box; Belongs to the helicases superfamily II, DEAD/DEAH box RNA helicase family, DEAD box subfamily; Localized in the cytoplasm; Family membership. | Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. | 0.785 |
| CAZ95123.1 | des6-2 | ZOBELLIA_1066 | ZOBELLIA_1067 | DEAD/DEAH RNA helicase; Protein that could be involved in ATP-dependent RNA unwinding in a variety of cellular processes, including ribosome assembly, protein synthesis, and RNA degradation; Contains a DEAD box; Belongs to the helicases superfamily II, DEAD/DEAH box RNA helicase family, DEAD box subfamily; Localized in the cytoplasm; Family membership. | Linoleoyl-CoA desaturase, also known as delta 6-desaturase, is responsible for the conversion of linoleic acid (18:2) to gamma-linolenic acid (18:3 gamma). It uses iron ion as a cofactor. Features five transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.785 |
| CAZ95123.1 | rpsE | ZOBELLIA_1066 | ZOBELLIA_2527 | DEAD/DEAH RNA helicase; Protein that could be involved in ATP-dependent RNA unwinding in a variety of cellular processes, including ribosome assembly, protein synthesis, and RNA degradation; Contains a DEAD box; Belongs to the helicases superfamily II, DEAD/DEAH box RNA helicase family, DEAD box subfamily; Localized in the cytoplasm; Family membership. | Ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family. | 0.662 |
| CAZ95123.1 | rpsL | ZOBELLIA_1066 | ZOBELLIA_2506 | DEAD/DEAH RNA helicase; Protein that could be involved in ATP-dependent RNA unwinding in a variety of cellular processes, including ribosome assembly, protein synthesis, and RNA degradation; Contains a DEAD box; Belongs to the helicases superfamily II, DEAD/DEAH box RNA helicase family, DEAD box subfamily; Localized in the cytoplasm; Family membership. | Ribosomal protein S12; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. | 0.415 |
| CAZ98902.1 | cspA1 | ZOBELLIA_4767 | ZOBELLIA_1065 | Conserved hypothetical protein. Localized in the cytoplasm. | Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. | 0.527 |
| CAZ98902.1 | rpoA | ZOBELLIA_4767 | ZOBELLIA_2535 | Conserved hypothetical protein. Localized in the cytoplasm. | DNA-dependent RNA polymerase, alpha subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.994 |
| CAZ98902.1 | rpoB | ZOBELLIA_4767 | ZOBELLIA_644 | Conserved hypothetical protein. Localized in the cytoplasm. | DNA-dependent RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.988 |
| CAZ98902.1 | rpsB | ZOBELLIA_4767 | ZOBELLIA_2345 | Conserved hypothetical protein. Localized in the cytoplasm. | The ribosomal protein S2 is a part of the ribosomal small subunit (30S) that contributes to the structural integrity of the ribosome; Belongs to the ribosomal protein S2p family; Localized in the cytoplasm; High confidence in function and specificity. | 0.964 |
| CAZ98902.1 | rpsE | ZOBELLIA_4767 | ZOBELLIA_2527 | Conserved hypothetical protein. Localized in the cytoplasm. | Ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family. | 0.560 |
| CAZ98902.1 | rpsL | ZOBELLIA_4767 | ZOBELLIA_2506 | Conserved hypothetical protein. Localized in the cytoplasm. | Ribosomal protein S12; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. | 0.863 |
| CAZ98902.1 | rpsT | ZOBELLIA_4767 | ZOBELLIA_2768 | Conserved hypothetical protein. Localized in the cytoplasm. | Ribosomal protein S20; Binds directly to 16S ribosomal RNA. | 0.723 |
| cspA1 | CAZ95123.1 | ZOBELLIA_1065 | ZOBELLIA_1066 | Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. | DEAD/DEAH RNA helicase; Protein that could be involved in ATP-dependent RNA unwinding in a variety of cellular processes, including ribosome assembly, protein synthesis, and RNA degradation; Contains a DEAD box; Belongs to the helicases superfamily II, DEAD/DEAH box RNA helicase family, DEAD box subfamily; Localized in the cytoplasm; Family membership. | 0.785 |
| cspA1 | CAZ98902.1 | ZOBELLIA_1065 | ZOBELLIA_4767 | Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. | Conserved hypothetical protein. Localized in the cytoplasm. | 0.527 |
| cspA1 | des6-2 | ZOBELLIA_1065 | ZOBELLIA_1067 | Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. | Linoleoyl-CoA desaturase, also known as delta 6-desaturase, is responsible for the conversion of linoleic acid (18:2) to gamma-linolenic acid (18:3 gamma). It uses iron ion as a cofactor. Features five transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.703 |
| cspA1 | rpmE | ZOBELLIA_1065 | ZOBELLIA_81 | Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. | Protein L31 is a part of the large subunit (50S) of the ribosome; Belongs to the ribosomal protein L31p family, type B subfamily; Localized in the cytoplasm; High confidence in function and specificity. | 0.467 |
| cspA1 | rpoA | ZOBELLIA_1065 | ZOBELLIA_2535 | Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. | DNA-dependent RNA polymerase, alpha subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.505 |
| cspA1 | rpoB | ZOBELLIA_1065 | ZOBELLIA_644 | Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. | DNA-dependent RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.524 |
| cspA1 | rpsB | ZOBELLIA_1065 | ZOBELLIA_2345 | Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. | The ribosomal protein S2 is a part of the ribosomal small subunit (30S) that contributes to the structural integrity of the ribosome; Belongs to the ribosomal protein S2p family; Localized in the cytoplasm; High confidence in function and specificity. | 0.412 |
| cspA1 | rpsE | ZOBELLIA_1065 | ZOBELLIA_2527 | Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. | Ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family. | 0.409 |
| cspA1 | rpsL | ZOBELLIA_1065 | ZOBELLIA_2506 | Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. | Ribosomal protein S12; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. | 0.454 |