| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EIC28037.1 | EIC28846.1 | Metal_0170 | Metal_1027 | PFAM: DSBA-like thioredoxin domain. | PFAM: Redoxin; TIGRFAM: periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily. | 0.504 |
| 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. | 0.722 |
| 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. | 0.433 |
| 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. | 0.982 |
| EIC28037.1 | dsbD | Metal_0170 | Metal_0063 | PFAM: DSBA-like thioredoxin domain. | Thiol:disulfide interchange protein; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. | 0.782 |
| EIC28037.1 | recG | Metal_0170 | Metal_1701 | PFAM: DSBA-like thioredoxin domain. | ATP-dependent DNA helicase RecG; Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y- DNA); Belongs to the helicase family. RecG subfamily. | 0.426 |
| 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. | 0.786 |
| EIC28457.1 | dsbD | Metal_0612 | Metal_0063 | 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. | Thiol:disulfide interchange protein; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. | 0.847 |
| EIC28846.1 | EIC28037.1 | Metal_1027 | Metal_0170 | PFAM: Redoxin; TIGRFAM: periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily. | PFAM: DSBA-like thioredoxin domain. | 0.504 |
| EIC28846.1 | dsbB | Metal_1027 | Metal_3356 | PFAM: Redoxin; TIGRFAM: periplasmic protein thiol:disulfide oxidoreductases, DsbE 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. | 0.574 |
| EIC28846.1 | dsbD | Metal_1027 | Metal_0063 | PFAM: Redoxin; TIGRFAM: periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily. | Thiol:disulfide interchange protein; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. | 0.934 |
| 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. | 0.596 |
| 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. | 0.722 |
| 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. | 0.786 |
| EIC30125.1 | dsbD | Metal_2402 | Metal_0063 | 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. | Thiol:disulfide interchange protein; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. | 0.847 |
| 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. | 0.646 |
| 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. | 0.614 |
| 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. | 0.433 |
| 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. | 0.614 |