| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo3085 | azo3087 | azo3085 | azo3087 | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | Conserved hypothetical protein. Homology to CV2710 of C.violaceum of 41% (trembl:Q7NUI8). Pfam: Hemerythrin HHE cation binding domain Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor MP2_NERDI binds Cadmium so as to protect the organism from toxicity. However Hemerythrin is classically described as Oxygen-binding through two at [...] | 0.951 |
| azo3085 | azo3096 | azo3085 | azo3096 | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein. | 0.693 |
| azo3085 | azo3098 | azo3085 | azo3098 | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | Putative Fnr-like transcriptional activator,; Function unclear. | 0.422 |
| azo3085 | ccoO | azo3085 | azo1342 | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl|Q8KS21). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...] | 0.971 |
| azo3085 | ccoP | azo3085 | azo1344 | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.639 |
| azo3085 | norB | azo3085 | azo3089 | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | Nitric-oxide reductase subunit B (EC 1.7.99.7) (Nitric oxide reductase cytochrome b subunit). 69% similarity to the P.stutzeri NorB protein. COMPONENT OF THE ANAEROBIC RESPIRATORY CHAIN THAT TRANSFORMS NITRATE TO DINITROGEN (DENITRIFICATION). NorB IS THE CATALYTIC SUBUNIT OF THE ENZYME COMPLEX. SHOWS PROTON PUMP ACTIVITY ACROSS THE MEMBRANE IN DENITRIFYING BACTERIAL CELLS. THE MONONITROGEN REDUCTION IS PROBABLY COUPLED TO ELECTRON TRANSPORT PHOSPHORYLATION.Belongs to the heme-copper respiratory oxidase family. Swiss Prot: Q59647. IPR000883; COX1. PF00115; COX1; 1. TMHMM:predicted trans [...] | 0.679 |
| azo3085 | norC | azo3085 | azo3088 | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | Nitric-oxide reductase subunit C (EC 1.7.99.7) (Nitric oxide reductase cytochrome c subunit) (NOR small subunit).COMPONENT OF THE ANAEROBIC RESPIRATORY CHAIN THAT TRANSFORMS NITRATE TO DINITROGEN (DENITRIFICATION).54% IPR000345; CytC_heme_BS. Pfam; PF00034; Cytochrom_C; 1. SignalP: present TMHelix:1; High confidence in function and specificity. | 0.872 |
| azo3087 | azo3085 | azo3087 | azo3085 | Conserved hypothetical protein. Homology to CV2710 of C.violaceum of 41% (trembl:Q7NUI8). Pfam: Hemerythrin HHE cation binding domain Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor MP2_NERDI binds Cadmium so as to protect the organism from toxicity. However Hemerythrin is classically described as Oxygen-binding through two at [...] | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | 0.951 |
| azo3087 | azo3096 | azo3087 | azo3096 | Conserved hypothetical protein. Homology to CV2710 of C.violaceum of 41% (trembl:Q7NUI8). Pfam: Hemerythrin HHE cation binding domain Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor MP2_NERDI binds Cadmium so as to protect the organism from toxicity. However Hemerythrin is classically described as Oxygen-binding through two at [...] | Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein. | 0.611 |
| azo3087 | azo3098 | azo3087 | azo3098 | Conserved hypothetical protein. Homology to CV2710 of C.violaceum of 41% (trembl:Q7NUI8). Pfam: Hemerythrin HHE cation binding domain Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor MP2_NERDI binds Cadmium so as to protect the organism from toxicity. However Hemerythrin is classically described as Oxygen-binding through two at [...] | Putative Fnr-like transcriptional activator,; Function unclear. | 0.413 |
| azo3087 | norB | azo3087 | azo3089 | Conserved hypothetical protein. Homology to CV2710 of C.violaceum of 41% (trembl:Q7NUI8). Pfam: Hemerythrin HHE cation binding domain Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor MP2_NERDI binds Cadmium so as to protect the organism from toxicity. However Hemerythrin is classically described as Oxygen-binding through two at [...] | Nitric-oxide reductase subunit B (EC 1.7.99.7) (Nitric oxide reductase cytochrome b subunit). 69% similarity to the P.stutzeri NorB protein. COMPONENT OF THE ANAEROBIC RESPIRATORY CHAIN THAT TRANSFORMS NITRATE TO DINITROGEN (DENITRIFICATION). NorB IS THE CATALYTIC SUBUNIT OF THE ENZYME COMPLEX. SHOWS PROTON PUMP ACTIVITY ACROSS THE MEMBRANE IN DENITRIFYING BACTERIAL CELLS. THE MONONITROGEN REDUCTION IS PROBABLY COUPLED TO ELECTRON TRANSPORT PHOSPHORYLATION.Belongs to the heme-copper respiratory oxidase family. Swiss Prot: Q59647. IPR000883; COX1. PF00115; COX1; 1. TMHMM:predicted trans [...] | 0.737 |
| azo3087 | norC | azo3087 | azo3088 | Conserved hypothetical protein. Homology to CV2710 of C.violaceum of 41% (trembl:Q7NUI8). Pfam: Hemerythrin HHE cation binding domain Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor MP2_NERDI binds Cadmium so as to protect the organism from toxicity. However Hemerythrin is classically described as Oxygen-binding through two at [...] | Nitric-oxide reductase subunit C (EC 1.7.99.7) (Nitric oxide reductase cytochrome c subunit) (NOR small subunit).COMPONENT OF THE ANAEROBIC RESPIRATORY CHAIN THAT TRANSFORMS NITRATE TO DINITROGEN (DENITRIFICATION).54% IPR000345; CytC_heme_BS. Pfam; PF00034; Cytochrom_C; 1. SignalP: present TMHelix:1; High confidence in function and specificity. | 0.668 |
| azo3096 | azo3085 | azo3096 | azo3085 | Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein. | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | 0.693 |
| azo3096 | azo3087 | azo3096 | azo3087 | Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein. | Conserved hypothetical protein. Homology to CV2710 of C.violaceum of 41% (trembl:Q7NUI8). Pfam: Hemerythrin HHE cation binding domain Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor MP2_NERDI binds Cadmium so as to protect the organism from toxicity. However Hemerythrin is classically described as Oxygen-binding through two at [...] | 0.611 |
| azo3096 | azo3098 | azo3096 | azo3098 | Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein. | Putative Fnr-like transcriptional activator,; Function unclear. | 0.833 |
| azo3096 | ccoN | azo3096 | azo1341 | Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein. | Probable cytochrome c oxidase, cbb3-type, subunit I. Homology to ccoN of R. capsulatus of 62% (sprot|COX1_RHOCA). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoN: cytochrome c oxidase cbb3-type Pfam: cytochrome c and quinol oxidase polyppeptide no signal peptide 12 TMHs; Hig [...] | 0.701 |
| azo3096 | ccoO | azo3096 | azo1342 | Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein. | Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl|Q8KS21). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...] | 0.794 |
| azo3096 | ccoP | azo3096 | azo1344 | Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein. | Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.790 |
| azo3096 | norB | azo3096 | azo3089 | Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein. | Nitric-oxide reductase subunit B (EC 1.7.99.7) (Nitric oxide reductase cytochrome b subunit). 69% similarity to the P.stutzeri NorB protein. COMPONENT OF THE ANAEROBIC RESPIRATORY CHAIN THAT TRANSFORMS NITRATE TO DINITROGEN (DENITRIFICATION). NorB IS THE CATALYTIC SUBUNIT OF THE ENZYME COMPLEX. SHOWS PROTON PUMP ACTIVITY ACROSS THE MEMBRANE IN DENITRIFYING BACTERIAL CELLS. THE MONONITROGEN REDUCTION IS PROBABLY COUPLED TO ELECTRON TRANSPORT PHOSPHORYLATION.Belongs to the heme-copper respiratory oxidase family. Swiss Prot: Q59647. IPR000883; COX1. PF00115; COX1; 1. TMHMM:predicted trans [...] | 0.741 |
| azo3096 | norC | azo3096 | azo3088 | Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein. | Nitric-oxide reductase subunit C (EC 1.7.99.7) (Nitric oxide reductase cytochrome c subunit) (NOR small subunit).COMPONENT OF THE ANAEROBIC RESPIRATORY CHAIN THAT TRANSFORMS NITRATE TO DINITROGEN (DENITRIFICATION).54% IPR000345; CytC_heme_BS. Pfam; PF00034; Cytochrom_C; 1. SignalP: present TMHelix:1; High confidence in function and specificity. | 0.658 |
