| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | azo3617 | azo0150 | azo3617 | 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 calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 0.572 |
| aas | ppiA | azo0150 | azo1057 | 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 [...] | Probable peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.599 |
| aas | ppiB | azo0150 | azo1056 | 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 [...] | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.599 |
| aas | rplB | azo0150 | azo3414 | 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 [...] | 50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family. | 0.598 |
| aas | rplO | azo0150 | azo3398 | 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 [...] | 50S ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family. | 0.602 |
| aas | rpsQ | azo0150 | azo3408 | 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 [...] | 30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.576 |
| azo1113 | azo1211 | azo1113 | azo1211 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 0.849 |
| azo1113 | azo2279 | azo1113 | azo2279 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 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 [...] | 0.907 |
| azo1113 | azo3617 | azo1113 | azo3617 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 0.835 |
| azo1113 | ppiA | azo1113 | azo1057 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | Probable peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.765 |
| azo1113 | ppiB | azo1113 | azo1056 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.765 |
| azo1113 | rplB | azo1113 | azo3414 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family. | 0.604 |
| azo1113 | rplO | azo1113 | azo3398 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 50S ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family. | 0.595 |
| azo1113 | rpsQ | azo1113 | azo3408 | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.500 |
| azo1211 | azo1113 | azo1211 | azo1113 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Conserved hypothetical protein. Homology to Bucepa03000705 of Burkholderia cepacia of 33% (gi|46323973|ref|ZP_00224335.1|(NBCI ENTREZ)). No domains predicted. No TMHs. No signal peptide. | 0.849 |
| azo1211 | azo2279 | azo1211 | azo2279 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 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 [...] | 0.899 |
| azo1211 | azo3617 | azo1211 | azo3617 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 0.945 |
| azo1211 | ppiA | azo1211 | azo1057 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Probable peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.925 |
| azo1211 | ppiB | azo1211 | azo1056 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.925 |