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Mettu_4189 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_4189" - TIGRFAM: RNA helicase, ATP-dependent DEAH box, HrpA type in Methylobacter tundripaludum
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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
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
Mettu_4189TIGRFAM- RNA helicase, ATP-dependent DEAH box, HrpA type; PFAM- Helicase-associated region; DNA/RNA helicase, C-terminal; Domain of unknown function DUF1605; KEGG- mca-MCA1482 ATP-dependent helicase HrpA; SMART- DEAD-like helicase, N-terminal; ATPase, AAA+ type, core; DNA/RNA helicase, C-terminal (1315 aa)    
Predicted Functional Partners:
Mettu_0730
KEGG- svo-SVI_3119 serine/threonine protein kinase; PFAM- Serine/threonine-protein kinase-like domain; Leucine-rich repeat; SMART- Serine/threonine-protein kinase domain; Tyrosine-protein kinase, subgroup, catalytic domain; Leucine-rich repeat, typical subtype (448 aa)
   
  0.937
pyrG
CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (543 aa)
     
 
    0.812
Mettu_0421
Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (193 aa)
       
  0.773
trmB
tRNA (guanine-N(7)-)-methyltransferase; Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA (229 aa)
 
      0.772
rtcA
RNA 3’-terminal phosphate cyclase; Catalyzes the conversion of 3’-phosphate to a 2’,3’- cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps- (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3’P to produce RNA- N3’PP5’A; (C) and attack of the adjacent 2’-hydroxyl on the 3’- phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (353 aa)
     
  0.751
Mettu_2595
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (694 aa)
     
  0.741
Mettu_1336
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (698 aa)
     
  0.741
Mettu_2829
30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence (553 aa)
   
  0.720
pcnB
Poly(A) polymerase I; Adds poly(A) tail to the 3’ end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control (467 aa)
 
      0.714
rpsD
30S ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit (206 aa)
     
  0.705
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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