| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AFN45764.1 | AFN46168.1 | HMPREF9154_2233 | HMPREF9154_2232 | Hypothetical protein. | Hypothetical protein. | 0.416 |
| AFN45764.1 | AFN46979.1 | HMPREF9154_2233 | HMPREF9154_2237 | Hypothetical protein. | UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family. | 0.495 |
| AFN45764.1 | adk | HMPREF9154_2233 | HMPREF9154_2235 | Hypothetical protein. | Adenylate kinase; 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. | 0.693 |
| AFN45764.1 | map_2 | HMPREF9154_2233 | HMPREF9154_2234 | Hypothetical protein. | Methionine aminopeptidase, type I; 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. | 0.693 |
| AFN45764.1 | secY | HMPREF9154_2233 | HMPREF9154_2236 | Hypothetical protein. | Preprotein translocase, SecY subunit; 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. | 0.693 |
| AFN46168.1 | AFN45764.1 | HMPREF9154_2232 | HMPREF9154_2233 | Hypothetical protein. | Hypothetical protein. | 0.416 |
| AFN46979.1 | AFN45764.1 | HMPREF9154_2237 | HMPREF9154_2233 | UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family. | Hypothetical protein. | 0.495 |
| AFN46979.1 | adk | HMPREF9154_2237 | HMPREF9154_2235 | UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family. | Adenylate kinase; 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. | 0.567 |
| AFN46979.1 | map_2 | HMPREF9154_2237 | HMPREF9154_2234 | UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family. | Methionine aminopeptidase, type I; 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. | 0.581 |
| AFN46979.1 | secY | HMPREF9154_2237 | HMPREF9154_2236 | UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family. | Preprotein translocase, SecY subunit; 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. | 0.547 |
| adk | AFN45764.1 | HMPREF9154_2235 | HMPREF9154_2233 | Adenylate kinase; 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. | Hypothetical protein. | 0.693 |
| adk | AFN46979.1 | HMPREF9154_2235 | HMPREF9154_2237 | Adenylate kinase; 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. | UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family. | 0.567 |
| adk | map_2 | HMPREF9154_2235 | HMPREF9154_2234 | Adenylate kinase; 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. | Methionine aminopeptidase, type I; 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. | 0.965 |
| adk | secY | HMPREF9154_2235 | HMPREF9154_2236 | Adenylate kinase; 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. | Preprotein translocase, SecY subunit; 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. | 0.995 |
| map_2 | AFN45764.1 | HMPREF9154_2234 | HMPREF9154_2233 | Methionine aminopeptidase, type I; 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. | Hypothetical protein. | 0.693 |
| map_2 | AFN46979.1 | HMPREF9154_2234 | HMPREF9154_2237 | Methionine aminopeptidase, type I; 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. | UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family. | 0.581 |
| map_2 | adk | HMPREF9154_2234 | HMPREF9154_2235 | Methionine aminopeptidase, type I; 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. | Adenylate kinase; 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. | 0.965 |
| map_2 | secY | HMPREF9154_2234 | HMPREF9154_2236 | Methionine aminopeptidase, type I; 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. | Preprotein translocase, SecY subunit; 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. | 0.971 |
| secY | AFN45764.1 | HMPREF9154_2236 | HMPREF9154_2233 | Preprotein translocase, SecY subunit; 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. | Hypothetical protein. | 0.693 |
| secY | AFN46979.1 | HMPREF9154_2236 | HMPREF9154_2237 | Preprotein translocase, SecY subunit; 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. | UDP-N-acetylglucosamine 2-epimerase; Belongs to the UDP-N-acetylglucosamine 2-epimerase family. | 0.547 |