node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ94370.1 | CAZ96747.1 | ZOBELLIA_297 | ZOBELLIA_2597 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | 0.953 |
CAZ94370.1 | CAZ98563.1 | ZOBELLIA_297 | ZOBELLIA_4428 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.960 |
CAZ94370.1 | rpsQ | ZOBELLIA_297 | ZOBELLIA_2519 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.907 |
CAZ94370.1 | sodA | ZOBELLIA_297 | ZOBELLIA_1583 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Superoxide dismutase [Mn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.488 |
CAZ94370.1 | ybeY | ZOBELLIA_297 | ZOBELLIA_1716 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Conserved hypothetical protein; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | 0.932 |
CAZ96747.1 | CAZ94370.1 | ZOBELLIA_2597 | ZOBELLIA_297 | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.953 |
CAZ96747.1 | CAZ98563.1 | ZOBELLIA_2597 | ZOBELLIA_4428 | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.959 |
CAZ96747.1 | rpsQ | ZOBELLIA_2597 | ZOBELLIA_2519 | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | Ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.907 |
CAZ96747.1 | sodA | ZOBELLIA_2597 | ZOBELLIA_1583 | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | Superoxide dismutase [Mn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.488 |
CAZ96747.1 | ybeY | ZOBELLIA_2597 | ZOBELLIA_1716 | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | Conserved hypothetical protein; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | 0.932 |
CAZ98563.1 | CAZ94370.1 | ZOBELLIA_4428 | ZOBELLIA_297 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.960 |
CAZ98563.1 | CAZ96747.1 | ZOBELLIA_4428 | ZOBELLIA_2597 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | 0.959 |
CAZ98563.1 | rpsQ | ZOBELLIA_4428 | ZOBELLIA_2519 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.907 |
CAZ98563.1 | sodA | ZOBELLIA_4428 | ZOBELLIA_1583 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Superoxide dismutase [Mn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.488 |
CAZ98563.1 | ybeY | ZOBELLIA_4428 | ZOBELLIA_1716 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Conserved hypothetical protein; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | 0.932 |
phoH | ybeY | ZOBELLIA_3833 | ZOBELLIA_1716 | PhoH is induced by phosphate starvation. It has an ATP-binding activity in vitro and is predicted to be a ATPase. Localized in the cytoplasm; Function unclear. | Conserved hypothetical protein; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | 0.870 |
rplK | rplO | ZOBELLIA_648 | ZOBELLIA_2529 | Ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family. | 0.989 |
rplK | rplQ | ZOBELLIA_648 | ZOBELLIA_2536 | Ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Ribosomal protein L17 is one of the proteins from the 50S ribosomal subunit; Belongs to a ribosomal proteins L17b/YmL8 (yeast) family; Localized in the cytoplasm; High confidence in function and specificity. | 0.988 |
rplK | rplU | ZOBELLIA_648 | ZOBELLIA_1359 | Ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.990 |
rplK | rpsQ | ZOBELLIA_648 | ZOBELLIA_2519 | Ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.988 |