| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| flgB | flgC | azo2740 | azo2739 | Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | 0.999 |
| flgB | flgE | azo2740 | azo2737 | Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar hook protein flgE. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | 0.998 |
| flgB | flgG | azo2740 | azo2735 | Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar basal-body rod protein flgG (Distal rod protein). The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | 0.997 |
| flgB | flgH | azo2740 | azo2734 | Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar L-ring protein precursor; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | 0.997 |
| flgB | flgI | azo2740 | azo2733 | Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar P-ring protein precursor; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | 0.996 |
| flgB | fliE | azo2740 | azo2713 | Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar hook-basal body complex protein FliE; Region start changed from 2997519 to 2997495 (-24 bases). | 0.997 |
| flgB | fliF | azo2740 | azo2716 | Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.997 |
| flgB | fliG | azo2740 | azo2717 | Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar motor switch protein fliG. FLIG IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE LOCATED AT THE BASE OF THE BASAL BODY. THIS COMPLEX INTERACTS WITH THE CHEY AND CHEZ CHEMOTAXIS PROTEINS IN ADDITION TO CONTACTING COMPONENTS OF THE MOTOR THAT DETERMINE THE DIRECTION OF FLAGELLAR ROTATION (BY SIMILARITY). fliG: flagellar motor switch protein Pfam: fliG C-terminal domain no signal peptide no TMHs; High confidence in function and specificity. | 0.982 |
| flgB | fliP | azo2740 | azo2726 | Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. | 0.995 |
| flgB | fliQ | azo2740 | azo2727 | Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar biosynthesis protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. | 0.994 |
| flgC | flgB | azo2739 | azo2740 | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.999 |
| flgC | flgE | azo2739 | azo2737 | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | Flagellar hook protein flgE. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | 0.999 |
| flgC | flgG | azo2739 | azo2735 | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | Flagellar basal-body rod protein flgG (Distal rod protein). The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | 0.997 |
| flgC | flgH | azo2739 | azo2734 | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | Flagellar L-ring protein precursor; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | 0.996 |
| flgC | flgI | azo2739 | azo2733 | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | Flagellar P-ring protein precursor; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | 0.996 |
| flgC | fliE | azo2739 | azo2713 | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | Flagellar hook-basal body complex protein FliE; Region start changed from 2997519 to 2997495 (-24 bases). | 0.994 |
| flgC | fliF | azo2739 | azo2716 | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | Flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.997 |
| flgC | fliG | azo2739 | azo2717 | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | Flagellar motor switch protein fliG. FLIG IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE LOCATED AT THE BASE OF THE BASAL BODY. THIS COMPLEX INTERACTS WITH THE CHEY AND CHEZ CHEMOTAXIS PROTEINS IN ADDITION TO CONTACTING COMPONENTS OF THE MOTOR THAT DETERMINE THE DIRECTION OF FLAGELLAR ROTATION (BY SIMILARITY). fliG: flagellar motor switch protein Pfam: fliG C-terminal domain no signal peptide no TMHs; High confidence in function and specificity. | 0.983 |
| flgC | fliP | azo2739 | azo2726 | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. | 0.995 |
| flgC | fliQ | azo2739 | azo2727 | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthesis protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. | 0.996 |