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secF protein (Acidaminococcus intestini) - STRING interaction network
"secF" - Protein-export membrane protein SecF in Acidaminococcus intestini
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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secFProtein-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 (295 aa)    
Predicted Functional Partners:
secD
Preprotein translocase subunit 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 (440 aa)
 
  0.999
queA
S-adenosylmethionine-tRNA-ribosyltransferase- isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA) (339 aa)
         
  0.856
yajC
Preprotein translocase subunit YajC (127 aa)
   
   
  0.812
tgt
Queuine tRNA-ribosyltransferase; Exchanges the guanine residue with 7-aminomethyl-7- deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis- dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (374 aa)
   
   
  0.805
Acin_0768
5-formyltetrahydrofolate cyclo-ligase (188 aa)
              0.785
secY
Preprotein translocase subunit secY; 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 (376 aa)
 
 
  0.780
ruvB
Holliday junction DNA helicase ruvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing (335 aa)
 
   
  0.754
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 super [...] (754 aa)
         
  0.706
ruvA
Holliday junction DNA helicase ruvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB (201 aa)
 
     
  0.675
Acin_0764
Hypothetical protein (440 aa)
              0.615
Your Current Organism:
Acidaminococcus intestini
NCBI taxonomy Id: 568816
Other names: A. intestini, A. intestini RyC-MR95, Acidaminococcus intestini, Acidaminococcus intestini Jumas-Bilak et al. 2007, Acidaminococcus intestini RyC-MR95, Acidaminococcus intestini strain RyC-MR95, Acidaminococcus sp. ADV 255.99
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