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
secDProtein-export membrane protein SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. (457 aa)    
Predicted Functional Partners:
secF
Protein-export membrane protein SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
0.999
Taci_0705
PFAM: 60 kDa inner membrane insertion protein; KEGG: dvu:DVU1077 inner membrane protein, 60 kDa.
  
 
 0.909
Taci_1218
TIGRFAM: preprotein translocase, YajC subunit; PFAM: YajC family protein; KEGG: mag:amb2515 preprotein translocase subunit YajC.
 
  
 0.902
secY
Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
 
 
 0.893
secE
Preprotein translocase, SecE subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
  
 
 0.848
pheT
KEGG: psa:PST_2364 phenylalanyl-tRNA synthetase subunit beta; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
 
 0.834
Taci_1214
PFAM: phosphoesterase RecJ domain protein; phosphoesterase DHHA1; KEGG: afw:Anae109_1327 single-stranded-DNA-specific exonuclease RecJ.
 
   
 0.634
Taci_1211
PFAM: beta-lactamase domain protein; KEGG: glo:Glov_3342 beta-lactamase domain protein.
     
 0.580
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...]
  
  
 0.572
metG
methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
 
 0.557
Your Current Organism:
Thermanaerovibrio acidaminovorans
NCBI taxonomy Id: 525903
Other names: T. acidaminovorans DSM 6589, Thermanaerovibrio acidaminovorans DSM 6589, Thermanaerovibrio acidaminovorans str. DSM 6589, Thermanaerovibrio acidaminovorans strain DSM 6589
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.