node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
TT_C0087 | TT_C1947 | TT_C0087 | TT_C1947 | annotation not available | annotation not available | 0.682 |
TT_C0087 | moeB | TT_C0087 | TT_C0979 | annotation not available | Molybdopterin-synthase adenylyltransferase; Adenylyltransferase involved in the biosynthesis of several sulfur compounds. Is required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2- thiouridine (m(5)s(2)U or s(2)T). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures. TtuC catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein TtuB. Is also involved in the biosynthesis of thiamine, mol [...] | 0.993 |
TT_C0087 | ttuA | TT_C0087 | TT_C0106 | annotation not available | TRNA-5-methyluridine54 2-sulfurtransferase; Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2- thiouridine (m(5)s(2)U or s(2)T) . This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is required for cell growth at high temperatures . TtuA transfers the S atom from the thiocarboxylated C-terminus of TtuB to tRNA | 0.666 |
TT_C0087 | ttuB | TT_C0087 | TT_C0105 | annotation not available | Sulfur carrier protein; Required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T) . This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures . Thiocarboxylated TtuB functions as the sulfur donor in the sulfurtransferase reaction catalyzed by TtuA TtuB also functions as a protein modifier covalently attached to lysine residues of the target proteins TtuA and TtuC . TtuB conjugation might play a regulatory role t [...] | 0.570 |
TT_C1133 | TT_C1835 | TT_C1133 | TT_C1835 | Hypothetical protein; Probable metalloprotease that cleaves the ubiquitin-like modifier protein TtuB from protein conjugates, hydrolyzing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. Does not seem to work for all the TtuB conjugates | annotation not available | 0.430 |
TT_C1133 | TT_C1947 | TT_C1133 | TT_C1947 | Hypothetical protein; Probable metalloprotease that cleaves the ubiquitin-like modifier protein TtuB from protein conjugates, hydrolyzing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. Does not seem to work for all the TtuB conjugates | annotation not available | 0.636 |
TT_C1133 | moeB | TT_C1133 | TT_C0979 | Hypothetical protein; Probable metalloprotease that cleaves the ubiquitin-like modifier protein TtuB from protein conjugates, hydrolyzing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. Does not seem to work for all the TtuB conjugates | Molybdopterin-synthase adenylyltransferase; Adenylyltransferase involved in the biosynthesis of several sulfur compounds. Is required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2- thiouridine (m(5)s(2)U or s(2)T). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures. TtuC catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein TtuB. Is also involved in the biosynthesis of thiamine, mol [...] | 0.815 |
TT_C1133 | ttuA | TT_C1133 | TT_C0106 | Hypothetical protein; Probable metalloprotease that cleaves the ubiquitin-like modifier protein TtuB from protein conjugates, hydrolyzing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. Does not seem to work for all the TtuB conjugates | TRNA-5-methyluridine54 2-sulfurtransferase; Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2- thiouridine (m(5)s(2)U or s(2)T) . This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is required for cell growth at high temperatures . TtuA transfers the S atom from the thiocarboxylated C-terminus of TtuB to tRNA | 0.560 |
TT_C1133 | ttuB | TT_C1133 | TT_C0105 | Hypothetical protein; Probable metalloprotease that cleaves the ubiquitin-like modifier protein TtuB from protein conjugates, hydrolyzing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. Does not seem to work for all the TtuB conjugates | Sulfur carrier protein; Required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T) . This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures . Thiocarboxylated TtuB functions as the sulfur donor in the sulfurtransferase reaction catalyzed by TtuA TtuB also functions as a protein modifier covalently attached to lysine residues of the target proteins TtuA and TtuC . TtuB conjugation might play a regulatory role t [...] | 0.799 |
TT_C1609 | moeB | TT_C1609 | TT_C0979 | Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for proces [...] | Molybdopterin-synthase adenylyltransferase; Adenylyltransferase involved in the biosynthesis of several sulfur compounds. Is required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2- thiouridine (m(5)s(2)U or s(2)T). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures. TtuC catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein TtuB. Is also involved in the biosynthesis of thiamine, mol [...] | 0.818 |
TT_C1835 | TT_C1133 | TT_C1835 | TT_C1133 | annotation not available | Hypothetical protein; Probable metalloprotease that cleaves the ubiquitin-like modifier protein TtuB from protein conjugates, hydrolyzing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. Does not seem to work for all the TtuB conjugates | 0.430 |
TT_C1835 | TT_C1947 | TT_C1835 | TT_C1947 | annotation not available | annotation not available | 0.945 |
TT_C1835 | moeB | TT_C1835 | TT_C0979 | annotation not available | Molybdopterin-synthase adenylyltransferase; Adenylyltransferase involved in the biosynthesis of several sulfur compounds. Is required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2- thiouridine (m(5)s(2)U or s(2)T). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures. TtuC catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein TtuB. Is also involved in the biosynthesis of thiamine, mol [...] | 0.938 |
TT_C1947 | TT_C0087 | TT_C1947 | TT_C0087 | annotation not available | annotation not available | 0.682 |
TT_C1947 | TT_C1133 | TT_C1947 | TT_C1133 | annotation not available | Hypothetical protein; Probable metalloprotease that cleaves the ubiquitin-like modifier protein TtuB from protein conjugates, hydrolyzing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. Does not seem to work for all the TtuB conjugates | 0.636 |
TT_C1947 | TT_C1835 | TT_C1947 | TT_C1835 | annotation not available | annotation not available | 0.945 |
TT_C1947 | moeA | TT_C1947 | TT_C1894 | annotation not available | Molybdopterin biosynthesis moea protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP | 0.942 |
TT_C1947 | moeB | TT_C1947 | TT_C0979 | annotation not available | Molybdopterin-synthase adenylyltransferase; Adenylyltransferase involved in the biosynthesis of several sulfur compounds. Is required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2- thiouridine (m(5)s(2)U or s(2)T). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures. TtuC catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein TtuB. Is also involved in the biosynthesis of thiamine, mol [...] | 0.999 |
TT_C1947 | thiG | TT_C1947 | TT_C0317 | annotation not available | Thiazole biosynthesis protein thig; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S | 0.619 |
moeA | TT_C1947 | TT_C1894 | TT_C1947 | Molybdopterin biosynthesis moea protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP | annotation not available | 0.942 |