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.
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Neighborhood
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[Homology]
Score
ctaECytochrome oxidase subunit III; PMID: 20576172 best DB hits: BLAST: embl:CAC08533.1; (AJ249578) cytochrome oxidase subunit III; E=3e-27 embl:CAA98149.1; (Z73914) ORF175 protein [Pseudomonas stutzeri]; E=2e-08 gb:AAG34379.1; AF197466_2 (AF197466) NirO [Pseudomonas; E=3e-08 COG: APE0793_2; COG1845 Heme/copper-type cytochrome/quinol oxidase,; E=5e-08 slr2083; COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit; E=8e-08 VNG0662G; COG1845 Heme/copper-type cytochrome/quinol oxidase,; E=2e-06. (431 aa)    
Predicted Functional Partners:
ctaC
Cytochrome oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
 
 0.999
ctaD
Cytochrome oxidase subunit I; PMID: 20576172 best DB hits: BLAST: embl:CAC08532.1; (AJ249578) cytochrome oxidase subunit I; E=1e-146 ddbj:BAA06976.1; (D32217) cytochrome c oxidase-like protein; E=1e-122 swissprot:Q06473; COX1_SYNY3 CYTOCHROME C OXIDASE POLYPEPTIDE I; E=3e-99 COG: slr1137; COG0843 Heme/copper-type cytochrome/quinol oxidases,; E=1e-100 RP405; COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit; E=3e-93 BS_ctaD; COG0843 Heme/copper-type cytochrome/quinol oxidases,; E=4e-91 PFAM: PF00115; Cytochrome C and Quinol oxidase pol; E=8.3e-185; Belongs to the heme-copper [...]
 
 0.999
RB4417
Cytochrome-c oxidase chain II/c precursor; PMID: 89231697 PMID: 91161592 best DB hits: BLAST: pir:A23711; cytochrome-c oxidase (EC 1.9.3.1) chain IIc precursor -; E=3e-42 swissprot:Q04441; COX2_BACFI CYTOCHROME C OXIDASE POLYPEPTIDE II; E=5e-38 ddbj:BAB06334.1; (AP001516) cytochrome caa3 oxidase (subunit II); E=2e-35 COG: BH2615_1; COG1622 Heme/copper-type cytochrome/quinol oxidases,; E=2e-21 XF1390; COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit; E=1e-14 slr1136; COG1622 Heme/copper-type cytochrome/quinol oxidases,; E=3e-14 PFAM: PF00116; Cytochrome C oxidase subunit II, [...]
 
 0.999
RB4416
Cytochrome c oxidase polypeptide I; PMID: 1847686 PMID: 94364936 PMID: 83257235 PMID: 88054981 best DB hits: BLAST: gb:AAD20227.1; (AF111945) quinol oxidase subunit I [Rhodobacter; E=1e-153 swissprot:P24010; COX1_BACSU CYTOCHROME C OXIDASE POLYPEPTIDE I; E=1e-102 pir:S14397; cytochrome-c oxidase (EC 1.9.3.1) chain I - Bacillus; E=1e-102 COG: BS_ctaD; COG0843 Heme/copper-type cytochrome/quinol oxidases,; E=1e-103 BH2614; COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit; E=1e-97 BS_qoxB; COG0843 Heme/copper-type cytochrome/quinol oxidases,; E=2e-90 PFAM: PF00115; Cytochrome C [...]
 
 0.997
cyoE
Protoheme IX farnesyltransferase; 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.
 
 
 0.995
ctaF
Similar to cytochrome oxidase subunit IV; PMID: 7678007 best DB hits: BLAST: embl:CAC08534.1; (AJ249578) cytochrome oxidase subunit IV; E=0.025.
 
 
 0.992
RB6350
PMID: 10984043 best DB hits: BLAST: pir:E83450; probable cytochrome oxidase subunit (cbb3-type) PA1557; E=1e-134 pir:E81050; cytochrome-c oxidase (EC 1.9.3.1) fixN chain NMB1725; E=1e-132 pir:C83452; probable cytochrome oxidase subunit (cbb3-type) PA1554; E=1e-129 COG: PA1557; COG3278 Cbb3-type cytochrome oxidase, subunit 1; E=1e-135 NMB1724; COG2993 Cbb3-type cytochrome oxidase, cytochrome c subunit; E=8e-38 slr1137; COG0843 Heme/copper-type cytochrome/quinol oxidases,; E=6e-12 PFAM: PF00115; Cytochrome C and Quinol oxidase poly; E=3.4e-65 PF02433; Cytochrome C oxidase, mono-heme subu [...]
  
 0.992
cox3
PMID: 2562384 best DB hits: BLAST: pir:A83632; cytochrome c oxidase, subunit III PA0108 [imported] -; E=6e-04 gb:AAG19157.1; (AE005013) cytochrome c oxidase subunit III; CoxC; E=0.007 gb:AAC09434.1; (M68929) coxIII [Marchantia polymorpha]; E=0.059 COG: PA0108; COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit; E=6e-05 VNG0662G; COG1845 Heme/copper-type cytochrome/quinol oxidase,; E=7e-04 PFAM: PF00510; Cytochrome c oxidase subunit III; E=0.55.
 
  
  0.965
nuoM
PMID: 7690854 best DB hits: BLAST: pir:H81796; NADH dehydrogenase (ubiquinone) (EC 1.6.5.3) chain M; E=1e-15 pir:E81220; NADH dehydrogenase I, M chain NMB0258 [imported] -; E=4e-15 swissprot:Q9ZCG0; NUOM_RICPR NADH DEHYDROGENASE I CHAIN M; E=3e-14 COG: NMB0258; COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M); E=4e-16 PH1431; COG0651 Formate hydrogenlyase subunit 3; E=6e-13 HP1272; COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M); E=3e-12 PFAM: PF00361; NADH-Ubiquinone/plastoquinone (co; E=2e-07.
   
 0.951
RB6353
PMID: 10952301 best DB hits: BLAST: pir:C82200; cytochrome c oxidase, chain CcoP VC1439 [similarity] -; E=7e-15 gb:AAB02559.1; (U58092) cbb3-type cytochrome c oxidase CcoP; E=1e-13 pir:A83452; probable cytochrome c PA1552 [imported] - Pseudomonas; E=1e-13 COG: VC1439; COG2010 Cytochrome c, mono- and diheme variants; E=7e-16 PFAM: PF00034; Cytochrome c; E=4.2e-11.
   
  0.933
Your Current Organism:
Rhodopirellula baltica
NCBI taxonomy Id: 243090
Other names: Pirellula sp. 1, R. baltica SH 1, Rhodopirellula baltica SH 1, Rhodopirellula baltica str. SH 1, Rhodopirellula baltica strain SH 1
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