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
Node Content
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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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
ADH59831.1KEGG: tpd:Teth39_0028 signal peptidase I; TIGRFAM: signal peptidase I; PFAM: Peptidase S24/S26A/S26B, conserved region; Belongs to the peptidase S26 family. (176 aa)    
Predicted Functional Partners:
lepA
GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
 
 
 0.811
ADH61541.1
KEGG: tpd:Teth39_0475 ATP dependent DNA ligase; TIGRFAM: DNA polymerase LigD, ligase domain protein; PFAM: ATP dependent DNA ligase.
   
  0.806
ADH61842.1
KEGG: ckr:CKR_2585 hypothetical protein; PFAM: RNA-metabolising metallo-beta-lactamase; SMART: beta-lactamase domain protein.
  
 
  0.801
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
  
 
 0.788
minE
Cell division topological specificity factor MinE; Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
  
    0.695
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]
     
 0.690
rnhB
Ribonuclease H; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
  
  
 0.690
ADH61273.1
KEGG: tpd:Teth39_0729 RNA polymerase, sigma 54 subunit, RpoN; TIGRFAM: RNA polymerase sigma-54 factor, RpoN; PFAM: sigma-54 DNA-binding domain protein; sigma-54 factor core-binding region; sigma-54 factor.
  
  
 0.594
ADH60961.1
TIGRFAM: membrane-associated zinc metalloprotease; PFAM: peptidase M50; PDZ/DHR/GLGF domain protein; KEGG: tpd:Teth39_1217 putative membrane-associated zinc metalloprotease; SMART: PDZ/DHR/GLGF domain protein.
 
  
 0.587
rnc
Ribonuclease III; Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
  
 
 0.573
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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