| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo0166 | azo0167 | azo0166 | azo0167 | Conserved hypothetical protein. Homology to ebA3023 of Azoarcus sp. EbN1 of 61% (trembl:Q5P4D4). No domains predicted. No TMHs. No signal peptide. | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | 0.734 |
| azo0166 | azo0168 | azo0166 | azo0168 | Conserved hypothetical protein. Homology to ebA3023 of Azoarcus sp. EbN1 of 61% (trembl:Q5P4D4). No domains predicted. No TMHs. No signal peptide. | Conserved hypothetical glutamine amidotransferases class-II (Gn-AT), YafJ-type. Homology to ebA3026 of Azoarcus sp. EbN1 of 75% (gnl|keqq|eba:ebA3026(KEGG)). Pfam: Glutamine amidotransferases class-II. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has an Ntn hydrolase; Conserved hypothetical protein. | 0.516 |
| azo0167 | azo0166 | azo0167 | azo0166 | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | Conserved hypothetical protein. Homology to ebA3023 of Azoarcus sp. EbN1 of 61% (trembl:Q5P4D4). No domains predicted. No TMHs. No signal peptide. | 0.734 |
| azo0167 | azo0168 | azo0167 | azo0168 | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | Conserved hypothetical glutamine amidotransferases class-II (Gn-AT), YafJ-type. Homology to ebA3026 of Azoarcus sp. EbN1 of 75% (gnl|keqq|eba:ebA3026(KEGG)). Pfam: Glutamine amidotransferases class-II. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has an Ntn hydrolase; Conserved hypothetical protein. | 0.585 |
| azo0167 | azo1250 | azo0167 | azo1250 | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | Conserved Hypotheitcal protein. Very strong consideration to be a homolog for SlyX protein. TrEMBL: Q7WMX4, 32% identity. Has PF04102|SlyX;(IPR007236):The SlyX protein has no known function. It is short less than 80 amino acids and is found close to the slyD gene. The SlyX protein has a conserved PPH(Y/W) motif at its C-terminus. The protein may be a coiled-coil structure. No Signal peptide present. No TMH present; Family membership. | 0.563 |
| azo0167 | azo2682 | azo0167 | azo2682 | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | Hypothetical protein predicted by Glimmer/Critica no homology to the data bank no domains predicted no signal peptide no TMHs. | 0.645 |
| azo0167 | azo2683 | azo0167 | azo2683 | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | Hypothetical protein predicted by Glimmer/Critica no homology to the data bank no domains predicted no signal peptide no TMHs. | 0.648 |
| azo0167 | fliG | azo0167 | azo2717 | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | 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. | 0.527 |
| azo0167 | fliM | azo0167 | azo2723 | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | Flagellar motor switch protein fliM. FLIM 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. InterPro: Flagellar motor switch protein FliM Pfam:Flagellar motor switch protein FliM no TMHs signale peptide: no analysis; High confidence in function and specificity. | 0.527 |
| azo0167 | rpoB | azo0167 | azo3424 | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | DNA-directed RNA polymerase; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.591 |
| azo0167 | rpoC | azo0167 | azo3423 | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | DNA-directed RNA polymerase; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.622 |
| azo0167 | rpoZ | azo0167 | azo3952 | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | DNA-directed RNA polymerase; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. | 0.596 |
| azo0168 | azo0166 | azo0168 | azo0166 | Conserved hypothetical glutamine amidotransferases class-II (Gn-AT), YafJ-type. Homology to ebA3026 of Azoarcus sp. EbN1 of 75% (gnl|keqq|eba:ebA3026(KEGG)). Pfam: Glutamine amidotransferases class-II. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has an Ntn hydrolase; Conserved hypothetical protein. | Conserved hypothetical protein. Homology to ebA3023 of Azoarcus sp. EbN1 of 61% (trembl:Q5P4D4). No domains predicted. No TMHs. No signal peptide. | 0.516 |
| azo0168 | azo0167 | azo0168 | azo0167 | Conserved hypothetical glutamine amidotransferases class-II (Gn-AT), YafJ-type. Homology to ebA3026 of Azoarcus sp. EbN1 of 75% (gnl|keqq|eba:ebA3026(KEGG)). Pfam: Glutamine amidotransferases class-II. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has an Ntn hydrolase; Conserved hypothetical protein. | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | 0.585 |
| azo1250 | azo0167 | azo1250 | azo0167 | Conserved Hypotheitcal protein. Very strong consideration to be a homolog for SlyX protein. TrEMBL: Q7WMX4, 32% identity. Has PF04102|SlyX;(IPR007236):The SlyX protein has no known function. It is short less than 80 amino acids and is found close to the slyD gene. The SlyX protein has a conserved PPH(Y/W) motif at its C-terminus. The protein may be a coiled-coil structure. No Signal peptide present. No TMH present; Family membership. | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | 0.563 |
| azo2682 | azo0167 | azo2682 | azo0167 | Hypothetical protein predicted by Glimmer/Critica no homology to the data bank no domains predicted no signal peptide no TMHs. | Conserved hypothetical protein; 55% HIT. Pfam:PF01230; HIT; 1. The Histidine Triad (HIT) motif, His-phi-His-phi-His-phi-phi (phi, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms. | 0.645 |
| azo2682 | azo2683 | azo2682 | azo2683 | Hypothetical protein predicted by Glimmer/Critica no homology to the data bank no domains predicted no signal peptide no TMHs. | Hypothetical protein predicted by Glimmer/Critica no homology to the data bank no domains predicted no signal peptide no TMHs. | 0.988 |
| azo2682 | rpoB | azo2682 | azo3424 | Hypothetical protein predicted by Glimmer/Critica no homology to the data bank no domains predicted no signal peptide no TMHs. | DNA-directed RNA polymerase; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.963 |
| azo2682 | rpoC | azo2682 | azo3423 | Hypothetical protein predicted by Glimmer/Critica no homology to the data bank no domains predicted no signal peptide no TMHs. | DNA-directed RNA polymerase; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.775 |
| azo2682 | rpoZ | azo2682 | azo3952 | Hypothetical protein predicted by Glimmer/Critica no homology to the data bank no domains predicted no signal peptide no TMHs. | DNA-directed RNA polymerase; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. | 0.962 |