| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| aas | ank1 | azo0150 | azo1599 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 0.641 |
| aas | azo0839 | azo0150 | azo0839 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 0.626 |
| aas | azo2279 | azo0150 | azo2279 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | 0.880 |
| aas | azo3172 | azo0150 | azo3172 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Putative long chain fatty acid coA ligase; It belongs to the ATP-dependent AMP-binding enzyme family. Entry name Q9X7Y5 Primary accession number Q9X7Y5 Identities = 193/609 (31%) InterPro IPR000873; AMP-bind. Pfam PF00501; AMP-binding; 2 Signal peptide probability: 0.006 Number of predicted TMHs: 0; Family membership. | 0.656 |
| aas | azo3685 | azo0150 | azo3685 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Putative hybrid sensor and regulator protein, MmoS) InterPro: IPR003594; ATPbind_ATPase. IPR005467; His_kinase. IPR003661; His_kinA_N. IPR008207; Hpt. IPR001610; PAC. IPR000700; PAS-assoc_C. IPR000014; PAS_domain. IPR001789; Response_reg. Pfam: PF02518; HATPase_c. PF00512; HisKA. PF00785; PAC. PF00989; PAS. PF00072; Response_reg. SMART: SM00387; HATPase_c. SM00388; HisKA. SM00073; HPT. SM00086; PAC. SM00091; PAS. SM00448; REC. TIGRFAM: TIGR00229; sensory_box. TMHMM reporting 2 transmembrane helices; Family membership. | 0.905 |
| aas | azo3776 | azo0150 | azo3776 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Conserved hypothetical membrane protein. Homology to ebA2790 of Azoarcus sp. EbN1 of 31% (gnl|keqq|eba:ebA2790(KEGG)). No domains predicted. no signal peptide. 2 TMHS; Conserved hypothetical protein. | 0.641 |
| aas | galE1 | azo0150 | azo3173 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | UDP-glucose 4-epimerase (EC 5.1.3.2) (Galactowaldenase) (UDP- galactose 4-epimerase). PLAYS AN ESSENTIAL ROLE IN THE INCORPORATION OF GALACTOSE INTO MENINGOCOCCAL LIPOPOLYSACCHARIDE SURFACE MOLECULES WHICH ARE IMPORTANT FOR PATHOGENESIS. hemL: glutamate-1-semialdehyde-21-amin; High confidence in function and specificity. | 0.781 |
| aas | tnkS | azo0150 | azo2985 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Putative tankyrase type protein; Tankyrase 2 (EC 2.4.2.30) (TANK2) (Tankyrase II) (TNKS-2) (TRF1- interacting ankyrin-related ADP-ribose polymerase 2) (Tankyrase-like protein) (Tankyrase-related protein). May regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. Has PARP activity and can modify TRF1 and thereby contribute to the regulation of telomere length. TREMBL:Q800E0:34%; Q8YTG9:36% identity. InterPro: Ankyrin-repeat Mop: molybdenum-pterin binding domain Presence of signal peptide (SignalP) but absence of transmembrane helices; Function [...] | 0.641 |
| alaS | ank1 | azo2780 | azo1599 | AlaS protein; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 0.838 |
| alaS | azo0839 | azo2780 | azo0839 | AlaS protein; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 0.799 |
| alaS | azo2279 | azo2780 | azo2279 | AlaS protein; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | 0.843 |
| alaS | azo3172 | azo2780 | azo3172 | AlaS protein; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Putative long chain fatty acid coA ligase; It belongs to the ATP-dependent AMP-binding enzyme family. Entry name Q9X7Y5 Primary accession number Q9X7Y5 Identities = 193/609 (31%) InterPro IPR000873; AMP-bind. Pfam PF00501; AMP-binding; 2 Signal peptide probability: 0.006 Number of predicted TMHs: 0; Family membership. | 0.666 |
| alaS | azo3776 | azo2780 | azo3776 | AlaS protein; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Conserved hypothetical membrane protein. Homology to ebA2790 of Azoarcus sp. EbN1 of 31% (gnl|keqq|eba:ebA2790(KEGG)). No domains predicted. no signal peptide. 2 TMHS; Conserved hypothetical protein. | 0.838 |
| alaS | tnkS | azo2780 | azo2985 | AlaS protein; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Putative tankyrase type protein; Tankyrase 2 (EC 2.4.2.30) (TANK2) (Tankyrase II) (TNKS-2) (TRF1- interacting ankyrin-related ADP-ribose polymerase 2) (Tankyrase-like protein) (Tankyrase-related protein). May regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. Has PARP activity and can modify TRF1 and thereby contribute to the regulation of telomere length. TREMBL:Q800E0:34%; Q8YTG9:36% identity. InterPro: Ankyrin-repeat Mop: molybdenum-pterin binding domain Presence of signal peptide (SignalP) but absence of transmembrane helices; Function [...] | 0.838 |
| ank1 | aas | azo1599 | azo0150 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | 0.641 |
| ank1 | alaS | azo1599 | azo2780 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | AlaS protein; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.838 |
| ank1 | azo0839 | azo1599 | azo0839 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 0.861 |
| ank1 | azo3172 | azo1599 | azo3172 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Putative long chain fatty acid coA ligase; It belongs to the ATP-dependent AMP-binding enzyme family. Entry name Q9X7Y5 Primary accession number Q9X7Y5 Identities = 193/609 (31%) InterPro IPR000873; AMP-bind. Pfam PF00501; AMP-binding; 2 Signal peptide probability: 0.006 Number of predicted TMHs: 0; Family membership. | 0.676 |
| azo0839 | aas | azo0839 | azo0150 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | 0.626 |
| azo0839 | alaS | azo0839 | azo2780 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | AlaS protein; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.799 |
