node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EIC28037.1 | EIC30125.1 | Metal_0170 | Metal_2402 | PFAM: DSBA-like thioredoxin domain. | Protein-disulfide isomerase; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. | 0.661 |
EIC28037.1 | cca | Metal_0170 | Metal_3358 | PFAM: DSBA-like thioredoxin domain. | tRNA nucleotidyltransferase/poly(A) polymerase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases. | 0.420 |
EIC28037.1 | dsbB | Metal_0170 | Metal_3356 | PFAM: DSBA-like thioredoxin domain. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.975 |
EIC28037.1 | lptD | Metal_0170 | Metal_2634 | PFAM: DSBA-like thioredoxin domain. | Organic solvent tolerance protein OstA; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. | 0.490 |
EIC28457.1 | dsbB | Metal_0612 | Metal_3356 | Disulfide bond isomerase protein; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.717 |
EIC29552.1 | cca | Metal_1785 | Metal_3358 | Flagellar basal-body rod protein FlgG; PFAM: Flagella basal body rod protein; Domain of unknown function (DUF1078); TIGRFAM: flagellar basal-body rod protein FlgB; fagellar hook-basal body proteins; flagellar basal-body rod protein FlgG, Gram-negative bacteria. | tRNA nucleotidyltransferase/poly(A) polymerase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases. | 0.470 |
EIC29552.1 | dsbB | Metal_1785 | Metal_3356 | Flagellar basal-body rod protein FlgG; PFAM: Flagella basal body rod protein; Domain of unknown function (DUF1078); TIGRFAM: flagellar basal-body rod protein FlgB; fagellar hook-basal body proteins; flagellar basal-body rod protein FlgG, Gram-negative bacteria. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.573 |
EIC30125.1 | EIC28037.1 | Metal_2402 | Metal_0170 | Protein-disulfide isomerase; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. | PFAM: DSBA-like thioredoxin domain. | 0.661 |
EIC30125.1 | dsbB | Metal_2402 | Metal_3356 | Protein-disulfide isomerase; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.717 |
EIC30125.1 | lptD | Metal_2402 | Metal_2634 | Protein-disulfide isomerase; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. | Organic solvent tolerance protein OstA; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. | 0.431 |
EIC30151.1 | dsbB | Metal_2429 | Metal_3356 | Hydro-lyase, Fe-S type, tartrate/fumarate subfamily; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.528 |
EIC30661.1 | EIC30662.1 | Metal_2981 | Metal_2982 | Putative enzyme of heme biosynthesis; PFAM: HemX; overlaps another CDS with the same product name. | Putative enzyme of heme biosynthesis; PFAM: HemY protein N-terminus; TIGRFAM: hemY protein; overlaps another CDS with the same product name. | 0.990 |
EIC30661.1 | dsbB | Metal_2981 | Metal_3356 | Putative enzyme of heme biosynthesis; PFAM: HemX; overlaps another CDS with the same product name. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.615 |
EIC30662.1 | EIC30661.1 | Metal_2982 | Metal_2981 | Putative enzyme of heme biosynthesis; PFAM: HemY protein N-terminus; TIGRFAM: hemY protein; overlaps another CDS with the same product name. | Putative enzyme of heme biosynthesis; PFAM: HemX; overlaps another CDS with the same product name. | 0.990 |
EIC30662.1 | dsbB | Metal_2982 | Metal_3356 | Putative enzyme of heme biosynthesis; PFAM: HemY protein N-terminus; TIGRFAM: hemY protein; overlaps another CDS with the same product name. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.531 |
EIC31020.1 | cca | Metal_3357 | Metal_3358 | Putative permease; PFAM: Sulfite exporter TauE/SafE. | tRNA nucleotidyltransferase/poly(A) polymerase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases. | 0.607 |
EIC31020.1 | dsbB | Metal_3357 | Metal_3356 | Putative permease; PFAM: Sulfite exporter TauE/SafE. | Disulfide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.651 |
cca | EIC28037.1 | Metal_3358 | Metal_0170 | tRNA nucleotidyltransferase/poly(A) polymerase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases. | PFAM: DSBA-like thioredoxin domain. | 0.420 |
cca | EIC29552.1 | Metal_3358 | Metal_1785 | tRNA nucleotidyltransferase/poly(A) polymerase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases. | Flagellar basal-body rod protein FlgG; PFAM: Flagella basal body rod protein; Domain of unknown function (DUF1078); TIGRFAM: flagellar basal-body rod protein FlgB; fagellar hook-basal body proteins; flagellar basal-body rod protein FlgG, Gram-negative bacteria. | 0.470 |
cca | EIC31020.1 | Metal_3358 | Metal_3357 | tRNA nucleotidyltransferase/poly(A) polymerase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases. | Putative permease; PFAM: Sulfite exporter TauE/SafE. | 0.607 |