node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MCBB_0907 | MCBB_0908 | MCBB_0907 | MCBB_0908 | Putative protein; tr|F6D239|F6D239_METPW;evalue=0.0; PctID=84.97; score=882; {ECO:0000313|EMBL:AEG17905,1}. | Putative conserved protein UCP037465, zinc finger protein, AF1427; tr|F6D240|F6D240_METPW;evalue=2e-030; PctID=81.16; score=137; {ECO:0000313|EMBL:AEG17906,1}. | 0.769 |
MCBB_0907 | aqpM | MCBB_0907 | MCBB_0909 | Putative protein; tr|F6D239|F6D239_METPW;evalue=0.0; PctID=84.97; score=882; {ECO:0000313|EMBL:AEG17905,1}. | Aquaporin AqpM; Channel that permits osmotically driven movement of water in both directions. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. Exhibits also a transient but reproducible increase in the initial glycerol flux (By similarity). three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA); sp|O26206|AQPM_METTH;evalue=2e-094; PctID=70.33; score=345. | 0.901 |
MCBB_0907 | msmS | MCBB_0907 | MCBB_1296 | Putative protein; tr|F6D239|F6D239_METPW;evalue=0.0; PctID=84.97; score=882; {ECO:0000313|EMBL:AEG17905,1}. | Heme-binding sensor kinase component part of a two-component regulatory system involved in methyl sulfide metabolism. Does not act as a phytochrome-like photoreceptor. phospho-L-histidine. Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Note=Heme-binding is redox-active and coordinates various ligands such as imidazole, dimethyl sulfide, and carbon monoxide depending on the redox state. The redox state of the heme cofactor influences on autophosphorylation activity: while reduced protein does not autophosphorylate, oxidized protein promotes autophosphorylation signal; redox state of heme [...] | 0.410 |
MCBB_0907 | pdtaS1 | MCBB_0907 | MCBB_0068 | Putative protein; tr|F6D239|F6D239_METPW;evalue=0.0; PctID=84.97; score=882; {ECO:0000313|EMBL:AEG17905,1}. | Putative sensor histidine kinase pdtaS; Member of the two-component regulatory system pdtaR/pdtaS. Autophosphorylates, probably on a histidine residue, and transfers its phosphate group to pdtaR (By similarity). phospho-L-histidine; sp|P9WGL4|PDTAS_MYCTO,sp|P9WGL5|PDTAS_MYCTU; evalue=2e-021; PctID=33.33; score=105. | 0.410 |
MCBB_0908 | MCBB_0907 | MCBB_0908 | MCBB_0907 | Putative conserved protein UCP037465, zinc finger protein, AF1427; tr|F6D240|F6D240_METPW;evalue=2e-030; PctID=81.16; score=137; {ECO:0000313|EMBL:AEG17906,1}. | Putative protein; tr|F6D239|F6D239_METPW;evalue=0.0; PctID=84.97; score=882; {ECO:0000313|EMBL:AEG17905,1}. | 0.769 |
MCBB_0908 | aqpM | MCBB_0908 | MCBB_0909 | Putative conserved protein UCP037465, zinc finger protein, AF1427; tr|F6D240|F6D240_METPW;evalue=2e-030; PctID=81.16; score=137; {ECO:0000313|EMBL:AEG17906,1}. | Aquaporin AqpM; Channel that permits osmotically driven movement of water in both directions. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. Exhibits also a transient but reproducible increase in the initial glycerol flux (By similarity). three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA); sp|O26206|AQPM_METTH;evalue=2e-094; PctID=70.33; score=345. | 0.854 |
aqpM | MCBB_0907 | MCBB_0909 | MCBB_0907 | Aquaporin AqpM; Channel that permits osmotically driven movement of water in both directions. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. Exhibits also a transient but reproducible increase in the initial glycerol flux (By similarity). three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA); sp|O26206|AQPM_METTH;evalue=2e-094; PctID=70.33; score=345. | Putative protein; tr|F6D239|F6D239_METPW;evalue=0.0; PctID=84.97; score=882; {ECO:0000313|EMBL:AEG17905,1}. | 0.901 |
aqpM | MCBB_0908 | MCBB_0909 | MCBB_0908 | Aquaporin AqpM; Channel that permits osmotically driven movement of water in both directions. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. Exhibits also a transient but reproducible increase in the initial glycerol flux (By similarity). three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA); sp|O26206|AQPM_METTH;evalue=2e-094; PctID=70.33; score=345. | Putative conserved protein UCP037465, zinc finger protein, AF1427; tr|F6D240|F6D240_METPW;evalue=2e-030; PctID=81.16; score=137; {ECO:0000313|EMBL:AEG17906,1}. | 0.854 |
msmS | MCBB_0907 | MCBB_1296 | MCBB_0907 | Heme-binding sensor kinase component part of a two-component regulatory system involved in methyl sulfide metabolism. Does not act as a phytochrome-like photoreceptor. phospho-L-histidine. Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Note=Heme-binding is redox-active and coordinates various ligands such as imidazole, dimethyl sulfide, and carbon monoxide depending on the redox state. The redox state of the heme cofactor influences on autophosphorylation activity: while reduced protein does not autophosphorylate, oxidized protein promotes autophosphorylation signal; redox state of heme [...] | Putative protein; tr|F6D239|F6D239_METPW;evalue=0.0; PctID=84.97; score=882; {ECO:0000313|EMBL:AEG17905,1}. | 0.410 |
msmS | pdtaS1 | MCBB_1296 | MCBB_0068 | Heme-binding sensor kinase component part of a two-component regulatory system involved in methyl sulfide metabolism. Does not act as a phytochrome-like photoreceptor. phospho-L-histidine. Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Note=Heme-binding is redox-active and coordinates various ligands such as imidazole, dimethyl sulfide, and carbon monoxide depending on the redox state. The redox state of the heme cofactor influences on autophosphorylation activity: while reduced protein does not autophosphorylate, oxidized protein promotes autophosphorylation signal; redox state of heme [...] | Putative sensor histidine kinase pdtaS; Member of the two-component regulatory system pdtaR/pdtaS. Autophosphorylates, probably on a histidine residue, and transfers its phosphate group to pdtaR (By similarity). phospho-L-histidine; sp|P9WGL4|PDTAS_MYCTO,sp|P9WGL5|PDTAS_MYCTU; evalue=2e-021; PctID=33.33; score=105. | 0.409 |
pdtaS1 | MCBB_0907 | MCBB_0068 | MCBB_0907 | Putative sensor histidine kinase pdtaS; Member of the two-component regulatory system pdtaR/pdtaS. Autophosphorylates, probably on a histidine residue, and transfers its phosphate group to pdtaR (By similarity). phospho-L-histidine; sp|P9WGL4|PDTAS_MYCTO,sp|P9WGL5|PDTAS_MYCTU; evalue=2e-021; PctID=33.33; score=105. | Putative protein; tr|F6D239|F6D239_METPW;evalue=0.0; PctID=84.97; score=882; {ECO:0000313|EMBL:AEG17905,1}. | 0.410 |
pdtaS1 | msmS | MCBB_0068 | MCBB_1296 | Putative sensor histidine kinase pdtaS; Member of the two-component regulatory system pdtaR/pdtaS. Autophosphorylates, probably on a histidine residue, and transfers its phosphate group to pdtaR (By similarity). phospho-L-histidine; sp|P9WGL4|PDTAS_MYCTO,sp|P9WGL5|PDTAS_MYCTU; evalue=2e-021; PctID=33.33; score=105. | Heme-binding sensor kinase component part of a two-component regulatory system involved in methyl sulfide metabolism. Does not act as a phytochrome-like photoreceptor. phospho-L-histidine. Name=heme; Xref=ChEBI:CHEBI:30413; Evidence=; Note=Heme-binding is redox-active and coordinates various ligands such as imidazole, dimethyl sulfide, and carbon monoxide depending on the redox state. The redox state of the heme cofactor influences on autophosphorylation activity: while reduced protein does not autophosphorylate, oxidized protein promotes autophosphorylation signal; redox state of heme [...] | 0.409 |