STRINGSTRING
Ndas_0404 Ndas_0404 Ndas_0405 Ndas_0405 Ndas_1214 Ndas_1214 Ndas_3016 Ndas_3016 Ndas_3136 Ndas_3136 Ndas_3325 Ndas_3325 Ndas_4112 Ndas_4112 nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD Ndas_5057 Ndas_5057 Ndas_5058 Ndas_5058 Ndas_5059 Ndas_5059 nuoH nuoH nuoI nuoI Ndas_5062 Ndas_5062 nuoK nuoK Ndas_5064 Ndas_5064 Ndas_5065 Ndas_5065 nuoN nuoN
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:
Ndas_0404Peptidase M16 domain protein; COGs: COG0612 Zn-dependent peptidase; InterPro IPR011237:IPR011249:IPR011765:IPR007863; KEGG: tfu:Tfu_2363 putative zinc proteinase; PFAM: peptidase M16 domain protein; SPTR: C1YLZ7 Predicted Zn-dependent peptidase; PFAM: Peptidase M16 inactive domain; Insulinase (Peptidase family M16). (442 aa)
Ndas_0405Peptidase M16 domain protein; COGs: COG0612 Zn-dependent peptidase; InterPro IPR011249:IPR011765:IPR007863:IPR011237; KEGG: tfu:Tfu_2362 putative proteinase; PFAM: peptidase M16 domain protein; SPTR: C1YLZ6 Predicted Zn-dependent peptidase; PFAM: Peptidase M16 inactive domain; Insulinase (Peptidase family M16). (449 aa)
Ndas_1214InterPro IPR006118; KEGG: hypothetical protein; SPTR: C1YTI6 Putative uncharacterized protein. (2922 aa)
Ndas_3016Rieske (2Fe-2S) iron-sulfur domain protein; COGs: COG2146 Ferredoxin subunits of nitrite reductase and ring-hydroxylating dioxygenase; InterPro IPR017941:IPR005805:IPR006311; KEGG: tfu:Tfu_2023 putative iron-sulphur protein; PFAM: Rieske [2Fe-2S] iron-sulphur domain; SPTR: C1YRS5 Ferredoxin subunit of nitrite reductase and ring-hydroxylating dioxygenase; PFAM: Rieske [2Fe-2S] domain; TIGRFAM: Tat (twin-arginine translocation) pathway signal sequence. (142 aa)
Ndas_3136Response regulator receiver protein; InterPro IPR001789:IPR011006; KEGG: tfu:Tfu_1023 putative response regulator; SMART: response regulator receiver; SPTR: C1YW44 Putative uncharacterized protein. (146 aa)
Ndas_3325KEGG: rmu:RMDY18_14720 ATP-dependent protease Clp, ATPase subunit; SPTR: C1YT36 Putative uncharacterized protein. (101 aa)
Ndas_4112Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; COGs: COG1894 NADH:ubiquinone oxidoreductase NADH-binding (51 kD) subunit; InterProIPR012335:IPR012336:IPR002023:IPR011538:IPR 019554:IPR019575:IPR001949; KEGG: sma:SAV_1835 NADH dehydrogenase I chain F; PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; NADH dehydrogenase (ubiquinone) 24 kDa subunit; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; SPTR: C1YSE4 NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit; PFAM: NADH-ubiquinone oxidoreductase-F iron [...] (656 aa)
nuoANADH-ubiquinone/plastoquinone oxidoreductase chain 3; 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. (121 aa)
nuoBNADH-quinone oxidoreductase, B subunit; 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. (181 aa)
nuoCNADH (or F420H2) dehydrogenase, subunit C; 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. (246 aa)
nuoDNADH dehydrogenase I, D subunit; 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. (431 aa)
Ndas_5057COGs: COG1905 NADH:ubiquinone oxidoreductase 24 kD subunit; InterPro IPR002023:IPR012336:IPR012335; KEGG: tfu:Tfu_2691 NADH dehydrogenase subunit E; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; SPTR: C1YIA8 NADH dehydrogenase subunit E; TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: Respiratory-chain NADH dehydrogenase 24 Kd subunit; TIGRFAM: NADH-quinone oxidoreductase, E subunit. (248 aa)
Ndas_5058NADH-quinone oxidoreductase, F subunit; 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. (439 aa)
Ndas_5059NADH-quinone oxidoreductase, chain G; 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. (830 aa)
nuoHNADH dehydrogenase (quinone); 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. (457 aa)
nuoINADH-quinone oxidoreductase, chain I; 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. (185 aa)
Ndas_5062NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. (349 aa)
nuoKNADH-ubiquinone oxidoreductase chain 4L; 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)
Ndas_5064Proton-translocating NADH-quinone oxidoreductase, chain L; COGs: COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter MnhA subunit; InterProIPR003945:IPR003916:IPR018393:IPR018486:IPR 001516:IPR001750; KEGG: tfu:Tfu_2684 NADH dehydrogenase subunit L; PFAM: NADH/Ubiquinone/plastoquinone (complex I); NADH-Ubiquinone oxidoreductase (complex I) chain 5/L domain protein; PRIAM: NADH dehydrogenase (quinone); SPTR: C1YIA1 NADH dehydrogenase subunit L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone/plastoquinone (c [...] (649 aa)
Ndas_5065Proton-translocating NADH-quinone oxidoreductase, chain M; COGs: COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M); InterPro IPR010227:IPR003918:IPR001750; KEGG: tfu:Tfu_2683 NADH dehydrogenase subunit M; PFAM: NADH/Ubiquinone/plastoquinone (complex I); SPTR: C1YIA0 NADH dehydrogenase subunit M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M. (555 aa)
nuoNProton-translocating NADH-quinone oxidoreductase, chain N; 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. (550 aa)
Your Current Organism:
Nocardiopsis dassonvillei
NCBI taxonomy Id: 446468
Other names: N. dassonvillei subsp. dassonvillei DSM 43111, Nocardiopsis dassonvillei DSM 43111, Nocardiopsis dassonvillei subsp. dassonvillei DSM 43111, Nocardiopsis dassonvillei subsp. dassonvillei str. DSM 43111, Nocardiopsis dassonvillei subsp. dassonvillei strain DSM 43111
Server load: medium (52%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.