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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
RB12666Best DB hits: BLAST: gb:AAB91057.1; (AE001094) molybdopterin oxidoreductase, iron-sulfur; E=5e-29 gb:AAG19285.1; (AE005024) molybdopterin oxidoreductase; HmoA; E=3e-26 gb:AAB90738.1; (AE001069) molybdopterin oxidoreductase, iron-sulfur; E=1e-24 COG: AF0175; COG0437 Fe-S-cluster-containing hydrogenase components 1; E=5e-30 PFAM: PF01568; Molydopterin dinucleotide bin; E=0.018 PF00037; 4Fe-4S binding domain; E=0.15. (1205 aa)    
Predicted Functional Partners:
RB12669
Best DB hits: BLAST: gb:AAB91058.1; (AE001094) molybdopterin oxidoreductase, membrane; E=5e-06 pir:T50876; hypothetical membrane protein [imported] - Rubrivivax; E=7e-06 gb:AAG19286.1; (AE005024) molybdopterin oxidoreductase; Moz; E=0.019.
 
 
 0.999
RB12664
Hypothetical protein-transmembrane prediction.
 
 
 0.996
RB12676
Hypothetical protein-signal peptide and transmembrane prediction; Best DB hits: PFAM: PF01473; Putative cell wall binding repea; E=0.31 PF02326; YMF19 hypothetical plant mitocho; E=0.59.
 
 
 0.991
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).
 
 
 
 0.980
RB12673
Hypothetical protein-transmembrane prediction.
 
 
 0.972
RB4408
Probable cytochrome c-552; PMID: 8973648 PMID: 91255245 best DB hits: BLAST: swissprot:P74917; C552_THIFE CYTOCHROME C-552 PRECURSOR (C552); E=8e-11 pir:B83334; probable cytochrome c PA2482 [imported] - Pseudomonas; E=5e-10 pir:F81040; cytochrome C4 NMB1805 [imported] - Neisseria; E=8e-10 COG: PA2482; COG2863 Cytochrome c553; E=4e-11 VC1439; COG2010 Cytochrome c, mono- and diheme variants; E=0.002.
  
 
 0.966
RB377
Molybdopterin oxidoreductase, iron sulfur subunit; PMID: 8635740 PMID: 1834669 best DB hits: BLAST: embl:CAC23825.1; (AL512979) molybdopterin oxidoreductase, iron; E=5e-26 gb:AAD37318.1; AF135170_9 (AF135170) dimethyl sulfoxide reductase; E=2e-25 swissprot:P18776; DMSB_ECOLI ANAEROBIC DIMETHYL SULFOXIDE; E=5e-25 COG: dmsB; COG0437 Fe-S-cluster-containing hydrogenase components 1; E=4e-26 TM0396; COG1142 Fe-S-cluster-containing hydrogenase components 2; E=5e-16 aq_067; COG0437 Fe-S-cluster-containing hydrogenase components 1; E=6e-16 PFAM: PF00037; 4Fe-4S binding domain; E=0.026.
 
 
0.961
RB524
Probable secreted glycosyl hydrolase; PMID: 8843436 best DB hits: BLAST: embl:CAB94634.1; (AL359215) putative secreted glycosyl hydrolase; E=1e-09 pir:T34929; hypothetical protein SC3F9.07 SC3F9.07 - Streptomyces; E=1e-04 embl:CAB55721.1; (AL117387) hypothetical protein SCF41.18; E=2e-04 PFAM: PF00034; Cytochrome c; E=0.0012.
  
 
 0.945
tufA
Translational elongation factor-Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.
  
 
 0.944
RB3953
PMID: 9923682 best DB hits: BLAST: pir:B71970; cytochrome oxidase (cbb3-type) - Helicobacter pylori; E=2e-04 pir:C64538; cytochrome-c oxidase (EC 1.9.3.1) chain fixP -; E=0.003 ddbj:BAA33529.1; (AB018105) cb-type cytochrome c oxidase subunit; E=0.009 COG: jhp0135; COG2010 Cytochrome c, mono- and diheme variants; E=2e-05 PFAM: PF00034; Cytochrome c; E=0.00073.
  
 
 0.943
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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