| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACE03846.1 | ACE03847.1 | Cphamn1_0901 | Cphamn1_0902 | Hypothetical protein. | KEGG: cch:Cag_0491 peptidase S26A, signal peptidase I; TIGRFAM: signal peptidase I; PFAM: peptidase S24 and S26 domain protein; Belongs to the peptidase S26 family. | 0.411 |
| ACE03846.1 | def | Cphamn1_0901 | Cphamn1_0898 | Hypothetical protein. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.477 |
| ACE03846.1 | fmt | Cphamn1_0901 | Cphamn1_0899 | Hypothetical protein. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.500 |
| ACE03846.1 | lepA | Cphamn1_0901 | Cphamn1_0900 | Hypothetical protein. | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.773 |
| ACE03847.1 | ACE03846.1 | Cphamn1_0902 | Cphamn1_0901 | KEGG: cch:Cag_0491 peptidase S26A, signal peptidase I; TIGRFAM: signal peptidase I; PFAM: peptidase S24 and S26 domain protein; Belongs to the peptidase S26 family. | Hypothetical protein. | 0.411 |
| ACE03847.1 | def | Cphamn1_0902 | Cphamn1_0898 | KEGG: cch:Cag_0491 peptidase S26A, signal peptidase I; TIGRFAM: signal peptidase I; PFAM: peptidase S24 and S26 domain protein; Belongs to the peptidase S26 family. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.603 |
| ACE03847.1 | fmt | Cphamn1_0902 | Cphamn1_0899 | KEGG: cch:Cag_0491 peptidase S26A, signal peptidase I; TIGRFAM: signal peptidase I; PFAM: peptidase S24 and S26 domain protein; Belongs to the peptidase S26 family. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.400 |
| ACE03847.1 | lepA | Cphamn1_0902 | Cphamn1_0900 | KEGG: cch:Cag_0491 peptidase S26A, signal peptidase I; TIGRFAM: signal peptidase I; PFAM: peptidase S24 and S26 domain protein; Belongs to the peptidase S26 family. | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.898 |
| def | ACE03846.1 | Cphamn1_0898 | Cphamn1_0901 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Hypothetical protein. | 0.477 |
| def | ACE03847.1 | Cphamn1_0898 | Cphamn1_0902 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | KEGG: cch:Cag_0491 peptidase S26A, signal peptidase I; TIGRFAM: signal peptidase I; PFAM: peptidase S24 and S26 domain protein; Belongs to the peptidase S26 family. | 0.603 |
| def | fmt | Cphamn1_0898 | Cphamn1_0899 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.966 |
| def | lepA | Cphamn1_0898 | Cphamn1_0900 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.618 |
| fmt | ACE03846.1 | Cphamn1_0899 | Cphamn1_0901 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Hypothetical protein. | 0.500 |
| fmt | ACE03847.1 | Cphamn1_0899 | Cphamn1_0902 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | KEGG: cch:Cag_0491 peptidase S26A, signal peptidase I; TIGRFAM: signal peptidase I; PFAM: peptidase S24 and S26 domain protein; Belongs to the peptidase S26 family. | 0.400 |
| fmt | def | Cphamn1_0899 | Cphamn1_0898 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.966 |
| fmt | lepA | Cphamn1_0899 | Cphamn1_0900 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.630 |
| lepA | ACE03846.1 | Cphamn1_0900 | Cphamn1_0901 | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | Hypothetical protein. | 0.773 |
| lepA | ACE03847.1 | Cphamn1_0900 | Cphamn1_0902 | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | KEGG: cch:Cag_0491 peptidase S26A, signal peptidase I; TIGRFAM: signal peptidase I; PFAM: peptidase S24 and S26 domain protein; Belongs to the peptidase S26 family. | 0.898 |
| lepA | def | Cphamn1_0900 | Cphamn1_0898 | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.618 |
| lepA | fmt | Cphamn1_0900 | Cphamn1_0899 | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.630 |