| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CPF_1992 | def-3 | CPF_1992 | CPF_1997 | Identified by match to protein family HMM PF00481. | 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. | 0.705 |
| CPF_1992 | fmt | CPF_1992 | CPF_1005 | Identified by match to protein family HMM PF00481. | 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. | 0.666 |
| CPF_1992 | fmt-2 | CPF_1992 | CPF_1996 | Identified by match to protein family HMM PF00481. | 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. | 0.868 |
| CPF_1992 | priA | CPF_1992 | CPF_1998 | Identified by match to protein family HMM PF00481. | Primosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.788 |
| CPF_1992 | sun | CPF_1992 | CPF_1994 | Identified by match to protein family HMM PF00481. | Ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.937 |
| def-3 | CPF_1992 | CPF_1997 | CPF_1992 | 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. | Identified by match to protein family HMM PF00481. | 0.705 |
| def-3 | fmt | CPF_1997 | CPF_1005 | 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. | 0.618 |
| def-3 | fmt-2 | CPF_1997 | CPF_1996 | 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. | 0.893 |
| def-3 | priA | CPF_1997 | CPF_1998 | 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. | Primosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.822 |
| def-3 | sun | CPF_1997 | CPF_1994 | 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. | Ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.804 |
| fhs | fmt | CPF_2785 | CPF_1005 | Formate--tetrahydrofolate ligase; Identified by similarity to SP:P13419; match to protein family HMM PF01268; Belongs to the formate--tetrahydrofolate ligase 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. | 0.921 |
| fhs | fmt-2 | CPF_2785 | CPF_1996 | Formate--tetrahydrofolate ligase; Identified by similarity to SP:P13419; match to protein family HMM PF01268; Belongs to the formate--tetrahydrofolate ligase 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. | 0.921 |
| fhs | purH | CPF_2785 | CPF_0677 | Formate--tetrahydrofolate ligase; Identified by similarity to SP:P13419; match to protein family HMM PF01268; Belongs to the formate--tetrahydrofolate ligase family. | Phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Identified by similarity to SP:P12048; match to protein family HMM PF01808; match to protein family HMM PF02142; match to protein family HMM TIGR00355. | 0.977 |
| fhs | purN | CPF_2785 | CPF_0676 | Formate--tetrahydrofolate ligase; Identified by similarity to SP:P13419; match to protein family HMM PF01268; Belongs to the formate--tetrahydrofolate ligase family. | Phosphoribosylglycinamide formyltransferase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. | 0.976 |
| fhs | sun | CPF_2785 | CPF_1994 | Formate--tetrahydrofolate ligase; Identified by similarity to SP:P13419; match to protein family HMM PF01268; Belongs to the formate--tetrahydrofolate ligase family. | Ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.591 |
| fmt | CPF_1992 | CPF_1005 | CPF_1992 | 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. | Identified by match to protein family HMM PF00481. | 0.666 |
| fmt | def-3 | CPF_1005 | CPF_1997 | 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. | 0.618 |
| fmt | fhs | CPF_1005 | CPF_2785 | 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. | Formate--tetrahydrofolate ligase; Identified by similarity to SP:P13419; match to protein family HMM PF01268; Belongs to the formate--tetrahydrofolate ligase family. | 0.921 |
| fmt | fmt-2 | CPF_1005 | CPF_1996 | 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. | 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. | 0.903 |
| fmt | metG | CPF_1005 | CPF_2846 | 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. | methionyl-tRNA synthetase; Identified by match to protein family HMM PF09334; match to protein family HMM TIGR00398. | 0.909 |