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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
dnaGDNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. (571 aa)    
Predicted Functional Partners:
rpoD
RNA polymerase sigma-70 factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
  
 0.980
dnaB
Replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins. Belongs to the helicase family. DnaB subfamily.
 0.957
der
GTPase family protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
  
  
 0.842
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
    
 
 0.820
rpoH
RNA polymerase sigma-32 factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes.
  
 0.799
rpsU
Ribosomal protein S21; Identified by similarity to SP:P02379; match to protein family HMM PF01165; match to protein family HMM TIGR00030; Belongs to the bacterial ribosomal protein bS21 family.
  
  
 0.748
gcp
O-sialoglycoprotein endopeptidase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction; Belongs to the KAE1 / TsaD family.
 
   
 0.739
polI
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
 
  
 0.732
MCA2992
GatB/Yqey domain protein; Identified by match to protein family HMM PF02637.
       0.674
MCA0769
Pyruvate ferredoxin/flavodoxin oxidoreductase family protein; Identified by similarity to SP:P52647; match to protein family HMM PF00037; match to protein family HMM PF01558; match to protein family HMM PF01855; match to protein family HMM PF02775; match to protein family HMM TIGR02176.
  
   0.637
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
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