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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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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[Homology]
Score
xth-1Exodeoxyribonuclease III; Identified by similarity to SP:P37454; match to protein family HMM PF03372; match to protein family HMM TIGR00195; match to protein family HMM TIGR00633. (257 aa)    
Predicted Functional Partners:
nth
Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate.
 
 0.978
xth-2
Exodeoxyribonuclease III; Identified by similarity to SP:P09030; match to protein family HMM PF03372; match to protein family HMM TIGR00195; match to protein family HMM TIGR00633.
  
  
 
0.925
dnaN
DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]
   
 0.838
hfq
Hfq protein; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Belongs to the Hfq family.
    
 
 0.801
MCA0320
Putative ampG protein; Identified by similarity to SP:P36670; match to protein family HMM PF07690.
       0.789
birA
birA bifunctional protein; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
  
    0.778
mutY
A/G-specific adenine glycosylase; Adenine glycosylase active on G-A mispairs.
    
 0.777
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.
  
 0.724
MCA0548
RNA pseudouridine synthase family protein; Identified by similarity to GP:9950157; match to protein family HMM PF00849; match to protein family HMM TIGR00093; Belongs to the pseudouridine synthase RsuA family.
  
    0.682
MCA2205
RNA pseudouridine synthase family protein; Identified by similarity to OMNI:NTL03PA03179; match to protein family HMM PF00849; match to protein family HMM TIGR00093; Belongs to the pseudouridine synthase RsuA family.
  
    0.682
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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