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Mettu_1255 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_1255" - KEGG: nwa:Nwat_2088 methylated-DNA/protein-cysteine methyltransferase in Methylobacter tundripaludum
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:
some 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 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_1255KEGG- nwa-Nwat_2088 methylated-DNA/protein-cysteine methyltransferase; TIGRFAM- Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding; PFAM- Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding (161 aa)    
Predicted Functional Partners:
xerD
TIGRFAM- Tyrosine recombinase XerD; HAMAP- Tyrosine recombinase xerD; KEGG- tgr-Tgr7_2127 tyrosine recombinase XerD; PFAM- Integrase, catalytic core, phage; Integrase, N-terminal SAM-like, phage (294 aa)
 
 
      0.917
Mettu_1253
TIGRFAM- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; KEGG- mca-MCA0397 UDP-N-acetylglucosamine acyltransferase; PFAM- Bacterial transferase hexapeptide repeat (257 aa)
              0.845
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
 
 
 
  0.736
Mettu_3580
Probable S-methyl-5’-thioinosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5’- thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1- phosphate. Involved in the breakdown of S-methyl-5’-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine (242 aa)
 
   
    0.705
Mettu_3755
RNA polymerase, sigma 32 subunit, RpoH; KEGG- nde-NIDE0990 RNA polymerase sigma factor RpoD (sigma-70); TIGRFAM- RNA polymerase sigma-70; PFAM- RNA polymerase sigma-70 region 4; RNA polymerase sigma-70 region 2; RNA polymerase sigma-70 region 3 (448 aa)
     
 
  0.653
rpoD
RNA polymerase sigma factor RpoD; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth (602 aa)
     
 
  0.653
rpoH
RNA polymerase sigma factor RpoH; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes (285 aa)
     
 
  0.625
rpoS
KEGG- alv-Alvin_0780 RNA polymerase sigma-70 subunit RpoD subfamily; TIGRFAM- RNA polymerase sigma factor RpoS, proteobacteria; RNA polymerase sigma-70; PFAM- RNA polymerase sigma-70 region 2; RNA polymerase sigma-70 region 1.2; RNA polymerase sigma-70 region 3; RNA polymerase sigma-70 region 4 (342 aa)
     
 
  0.611
Mettu_2662
KEGG- RNA polymerase, sigma 70 subunit, RpoD subfamily; TIGRFAM- RNA polymerase sigma-70; PFAM- RNA polymerase sigma-70 region 4; RNA polymerase sigma-70 region 2; Belongs to the sigma-70 factor family (391 aa)
     
 
  0.611
Mettu_1576
Outer membrane adhesin like proteiin; TIGRFAM- VCBS repeat domain; PFAM- Putative Ig; KEGG- cch-Cag_1242 VCBS; SMART- Dystroglycan-type cadherin-like (6210 aa)
   
        0.608
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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