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STRINGSTRING
Mettu_2037 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2037" - PFAM: Aminoglycoside phosphotransferase in Methylobacter tundripaludum
Nodes:
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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
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proteins of unknown 3D structure
filled nodes:
some 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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Mettu_2037PFAM- Aminoglycoside phosphotransferase; KEGG- npu-Npun_R1422 aminoglycoside phosphotransferase (354 aa)    
Predicted Functional Partners:
Mettu_1405
Methionine synthase; TIGRFAM- 5-methyltetrahydrofolate--homocysteine methyltransferase; KEGG- mca-MCA1545 B12-dependent methionine synthase; PFAM- Homocysteine S-methyltransferase; Dihydropteroate synthase, DHPS; Methionine synthase, cobalamin (vitamin B12)-binding module, cap; Cobalamin (vitamin B12)-binding; Vitamin B12 dependent methionine synthase, activation region (1226 aa)
   
 
  0.806
Mettu_2036
KEGG- nhl-Nhal_0414 hypothetical protein (464 aa)
 
          0.558
Mettu_2038
dITP/XTP pyrophosphatase; 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 (203 aa)
   
        0.531
rph
Ribonuclease PH; Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates (345 aa)
              0.512
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
         
  0.497
Mettu_1040
KEGG- mca-MCA0597 homoserine dehydrogenase; PFAM- Homoserine dehydrogenase, catalytic; Aspartate/homoserine dehydrogenase, NAD-binding; Amino acid-binding ACT (436 aa)
   
 
  0.422
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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