STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
KIR63369.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (273 aa)    
Predicted Functional Partners:
KIR60994.1
Cytochrome B561; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.929
ctaB
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.
 
 
 0.751
CoxB
Cytochrome C 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).
 
 
 0.690
secY
Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
   
   0.651
CtaD
Cytochrome C oxidase subunit I; 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.
 
 
 0.618
CtaD-2
Cytochrome C oxidase subunit I; 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.
 
 
 0.617
KIR60808.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.609
KIR65275.1
RCC1 repeats protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
   0.601
KIR60810.1
(2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.581
KIR64524.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.515
Your Current Organism:
Micromonospora carbonacea
NCBI taxonomy Id: 47853
Other names: ATCC 27114, ATCC 27115, DSM 43168, DSM 43815, IFO 14107, IFO 14108, JCM 3139, M. carbonacea, Micromonospora carbonacea subsp. aurantiaca, Micromonospora carbonacea subsp. carbonacea, NBRC 14108, NRRL 2972
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