node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OGY59204.1 | OGY59345.1 | A3F24_01675 | A3F24_00650 | Ribonucleoside-diphosphate reductase; Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen. | Ribonucleoside-diphosphate reductase subunit alpha; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | 0.955 |
OGY59204.1 | adk | A3F24_01675 | A3F24_01020 | Ribonucleoside-diphosphate reductase; Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen. | Hypothetical protein; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family. | 0.941 |
OGY59345.1 | OGY59204.1 | A3F24_00650 | A3F24_01675 | Ribonucleoside-diphosphate reductase subunit alpha; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | Ribonucleoside-diphosphate reductase; Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen. | 0.955 |
OGY59345.1 | adk | A3F24_00650 | A3F24_01020 | Ribonucleoside-diphosphate reductase subunit alpha; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | Hypothetical protein; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family. | 0.941 |
OGY59726.1 | OGY59727.1 | A3F24_00990 | A3F24_00995 | 30S ribosomal protein S8; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | 0.999 |
OGY59726.1 | OGY59729.1 | A3F24_00990 | A3F24_01005 | 30S ribosomal protein S8; Derived by automated computational analysis using gene prediction method: Protein Homology. | 30S ribosomal protein S5; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uS5 family. | 0.999 |
OGY59726.1 | adk | A3F24_00990 | A3F24_01020 | 30S ribosomal protein S8; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family. | 0.859 |
OGY59726.1 | map | A3F24_00990 | A3F24_01025 | 30S ribosomal protein S8; Derived by automated computational analysis using gene prediction method: Protein Homology. | Type I methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.999 |
OGY59726.1 | rplO | A3F24_00990 | A3F24_01010 | 30S ribosomal protein S8; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family. | 0.999 |
OGY59726.1 | rplR | A3F24_00990 | A3F24_01000 | 30S ribosomal protein S8; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L18; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | 0.999 |
OGY59726.1 | rpsZ | A3F24_00990 | A3F24_00985 | 30S ribosomal protein S8; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L5; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. | 0.999 |
OGY59726.1 | secY | A3F24_00990 | A3F24_01015 | 30S ribosomal protein S8; Derived by automated computational analysis using gene prediction method: Protein Homology. | Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.999 |
OGY59727.1 | OGY59726.1 | A3F24_00995 | A3F24_00990 | 50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | 30S ribosomal protein S8; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
OGY59727.1 | OGY59729.1 | A3F24_00995 | A3F24_01005 | 50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | 30S ribosomal protein S5; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uS5 family. | 0.999 |
OGY59727.1 | adk | A3F24_00995 | A3F24_01020 | 50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | Hypothetical protein; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family. | 0.856 |
OGY59727.1 | map | A3F24_00995 | A3F24_01025 | 50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | Type I methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.999 |
OGY59727.1 | rplO | A3F24_00995 | A3F24_01010 | 50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | Hypothetical protein; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family. | 0.999 |
OGY59727.1 | rplR | A3F24_00995 | A3F24_01000 | 50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | 50S ribosomal protein L18; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | 0.999 |
OGY59727.1 | rpsZ | A3F24_00995 | A3F24_00985 | 50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | 50S ribosomal protein L5; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. | 0.999 |
OGY59727.1 | secY | A3F24_00995 | A3F24_01015 | 50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.999 |