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pdtaS5 pdtaS5 pdtaS15 pdtaS15 pdtaS9 pdtaS9 pdtaR7 pdtaR7 msmS msmS
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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experimentally determined
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textmining
co-expression
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Your Input:
pdtaS5Putative 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=4e-017; PctID=31.94; score=91.3. (991 aa)
pdtaS15Putative 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=1e-016; PctID=30.43; score=87.8. (373 aa)
pdtaS9Putative 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-020; PctID=32.98; score=102. (750 aa)
pdtaR7Putative transcriptional regulatory protein pdtaR; Member of the two-component regulatory system pdtaR/pdtaS. (Potential). ProRule:PRU00308}. Sequence=AAK45932.1; Type=Erroneous initiation; Evidence=; sp|P9WGM2|PDTAR_MYCTO,sp|P9WGM3|PDTAR_MYCTU; evalue=1e-014; PctID=35.77; score=83.2. (1022 aa)
msmSHeme-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 [...] (751 aa)
Your Current Organism:
Methanobacterium congolense
NCBI taxonomy Id: 118062
Other names: DSM 7095, M. congolense, Methanobacterium congolense Cuzin et al. 2001, OCM 786, strain C
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