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.
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experimentally determined
co-expression
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gene co-occurrence
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Score
ADH61771.1PHP domain protein; KEGG: tex:Teth514_0650 phosphotransferase domain-containing protein; PFAM: PHP domain protein; SMART: DNA polymerase X; phosphoesterase PHP domain protein; Helix-hairpin-helix DNA-binding class 1. (570 aa)    
Predicted Functional Partners:
ADH61541.1
KEGG: tpd:Teth39_0475 ATP dependent DNA ligase; TIGRFAM: DNA polymerase LigD, ligase domain protein; PFAM: ATP dependent DNA ligase.
  
 0.950
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
   
 0.941
ADH59791.1
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 [...]
    
 0.743
hisI
phosphoribosyl-ATP diphosphatase; KEGG: tpd:Teth39_0522 bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP pyrophosphatase protein; TIGRFAM: phosphoribosyl-ATP diphosphatase; PFAM: phosphoribosyl-AMP cyclohydrolase; phosphoribosyl-ATP pyrophosphohydrolase; In the N-terminal section; belongs to the PRA-CH family.
  
  
 0.710
mutS2
MutS2 family protein; Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity; Belongs to the DNA mismatch repair MutS family. MutS2 subfamily.
  
  
 0.678
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.
     
 0.599
ADH60570.1
Signal peptide peptidase SppA, 36K type; KEGG: tte:TTE0850 periplasmic serine protease (ClpP class); TIGRFAM: signal peptide peptidase SppA, 36K type; PFAM: peptidase S49.
 
     0.512
ADH61261.1
PFAM: protein of unknown function DUF34; KEGG: tpd:Teth39_0741 hypothetical protein; Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
 
    0.486
ADH61329.1
DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein; TIGRFAM: DNA polymerase III, alpha subunit; KEGG: tex:Teth514_1192 DNA polymerase III DnaE; PFAM: DNA polymerase III alpha subunit; nucleic acid binding OB-fold tRNA/helicase-type; PHP domain protein.
     
 0.470
uvrC
Excinuclease ABC, C subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
  
  
 0.451
Your Current Organism:
Thermoanaerobacter mathranii
NCBI taxonomy Id: 583358
Other names: T. mathranii subsp. mathranii str. A3, Thermoanaerobacter mathranii subsp. mathranii A3, Thermoanaerobacter mathranii subsp. mathranii DSM 11426, Thermoanaerobacter mathranii subsp. mathranii str. A3, Thermoanaerobacter mathranii subsp. mathranii strain A3
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