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
dutDeoxyuridine 5'-triphosphate nucleotidohydrolase Dut; This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family. (148 aa)    
Predicted Functional Partners:
tdk
KEGG: tpd:Teth39_2112 thymidine kinase; PFAM: thymidine kinase.
   
 
 0.960
tmk
Thymidylate kinase; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis; Belongs to the thymidylate kinase family.
  
 
 0.950
ADH60409.1
Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
  
 0.940
ADH61357.1
KEGG: tpd:Teth39_0653 anaerobic ribonucleoside triphosphate reductase; TIGRFAM: anaerobic ribonucleoside-triphosphate reductase; PFAM: ATP-cone domain protein.
    
 0.937
ADH59972.1
PFAM: CMP/dCMP deaminase zinc-binding; KEGG: tpd:Teth39_2103 CMP/dCMP deaminase, zinc-binding.
  
 0.933
ndk
Nucleoside-diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family.
   
 
 0.922
surE
Stationary-phase survival protein SurE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family.
    
 0.915
ADH60156.1
5'-Nucleotidase domain protein; KEGG: tpd:Teth39_1938 5'-nucleotidase, 2',3'-cyclic-nucleotide 2'-phosphodiesterase; PFAM: 5'-Nucleotidase domain protein; SH3 type 3 domain protein; metallophosphoesterase; SMART: SH3 domain protein; Capsule synthesis protein, CapA.
    
  0.900
ADH61079.1
Phosphopantothenoylcysteine decarboxylase/phosphopantothenate/cysteine ligase; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family.
 
 
 0.898
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 [...]
  
  
 0.830
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
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.