STRINGSTRING
D0Z67_14250 D0Z67_14250 coxB coxB GCA_000725795_01070 GCA_000725795_01070 D0Z67_07600 D0Z67_07600 D0Z67_07590 D0Z67_07590 D0Z67_07585 D0Z67_07585 D0Z67_07580 D0Z67_07580 D0Z67_07575 D0Z67_07575 D0Z67_07570 D0Z67_07570 D0Z67_04155 D0Z67_04155 D0Z67_13060 D0Z67_13060 D0Z67_01970 D0Z67_01970 D0Z67_18195 D0Z67_18195 nuoN nuoN D0Z67_17025 D0Z67_17025 D0Z67_17020 D0Z67_17020 nuoK nuoK D0Z67_17010 D0Z67_17010 nuoI nuoI nuoH nuoH D0Z67_16995 D0Z67_16995 nuoB nuoB D0Z67_16985 D0Z67_16985 D0Z67_18910 D0Z67_18910 D0Z67_25275 D0Z67_25275 ctaD ctaD D0Z67_25070 D0Z67_25070 D0Z67_22590 D0Z67_22590 ctaB ctaB D0Z67_06480 D0Z67_06480 D0Z67_06085 D0Z67_06085 D0Z67_26840 D0Z67_26840 D0Z67_10600 D0Z67_10600 nuoD nuoD D0Z67_06600 D0Z67_06600 nuoN-2 nuoN-2 D0Z67_16850 D0Z67_16850 D0Z67_16845 D0Z67_16845 nuoK-2 nuoK-2 D0Z67_16835 D0Z67_16835 nuoI-2 nuoI-2 nuoH-2 nuoH-2 D0Z67_16820 D0Z67_16820 nuoF nuoF nuoE nuoE nuoD-2 nuoD-2 nuoC nuoC nuoB-2 nuoB-2 nuoA nuoA D0Z67_22245 D0Z67_22245 D0Z67_22240 D0Z67_22240 D0Z67_22235 D0Z67_22235 D0Z67_09290 D0Z67_09290
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
D0Z67_14250Unannotated protein. (150 aa)
coxBUnannotated protein. (330 aa)
GCA_000725795_01070Unannotated protein. (67 aa)
D0Z67_07600Unannotated protein; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. (132 aa)
D0Z67_07590Unannotated protein. (133 aa)
D0Z67_07585Unannotated protein. (206 aa)
D0Z67_07580Unannotated protein. (270 aa)
D0Z67_07575Unannotated protein. (352 aa)
D0Z67_07570Unannotated protein. (545 aa)
D0Z67_04155Unannotated protein. (246 aa)
D0Z67_13060Unannotated protein. (336 aa)
D0Z67_01970Unannotated protein. (285 aa)
D0Z67_18195Unannotated protein. (253 aa)
nuoNUnannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. (507 aa)
D0Z67_17025Unannotated protein. (516 aa)
D0Z67_17020Unannotated protein. (664 aa)
nuoKUnannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family. (126 aa)
D0Z67_17010Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (199 aa)
nuoIUnannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (189 aa)
nuoHUnannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. (322 aa)
D0Z67_16995Unannotated protein. (453 aa)
nuoBUnannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (201 aa)
D0Z67_16985Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (138 aa)
D0Z67_18910Unannotated protein. (463 aa)
D0Z67_25275Unannotated protein. (268 aa)
ctaDUnannotated protein; 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 are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (648 aa)
D0Z67_25070Unannotated protein. (246 aa)
D0Z67_22590Unannotated protein. (192 aa)
ctaBUnannotated protein; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (333 aa)
D0Z67_06480Unannotated protein. (336 aa)
D0Z67_06085Unannotated protein. (265 aa)
D0Z67_26840Unannotated protein. (209 aa)
D0Z67_10600Unannotated protein. (100 aa)
nuoDUnannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. (382 aa)
D0Z67_06600Unannotated protein. (124 aa)
nuoN-2Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. (549 aa)
D0Z67_16850Unannotated protein. (525 aa)
D0Z67_16845Unannotated protein. (631 aa)
nuoK-2Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family. (99 aa)
D0Z67_16835Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (280 aa)
nuoI-2Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (209 aa)
nuoH-2Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. (453 aa)
D0Z67_16820Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. (834 aa)
nuoFUnannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (449 aa)
nuoEUnannotated protein. (285 aa)
nuoD-2Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. (440 aa)
nuoCUnannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family. (247 aa)
nuoB-2Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (184 aa)
nuoAUnannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. (119 aa)
D0Z67_22245Unannotated protein. (247 aa)
D0Z67_22240Unannotated protein. (462 aa)
D0Z67_22235Unannotated protein. (464 aa)
D0Z67_09290Unannotated protein. (536 aa)
Your Current Organism:
Streptomyces seoulensis
NCBI taxonomy Id: 73044
Other names: CIP 105312, IFO 16255, IFO 16668, IMSNU 21266, JCM 10116, NBRC 16255, NBRC 16668, S. seoulensis, Streptomyces sp. USC028, Streptomyces sp. USC046, strain IMSNU-1
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