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
MMP0988RNA methyltransferase related protein; Citation: J Mol Microbiol Biotechnol. 2002 Jan;4(1):71-5. (295 aa)    
Predicted Functional Partners:
thyA
Thymidylate synthase; Citation: Xu et al., Nature Structural. Biol. 6, 750 (1999).
 
    0.833
rsmA
Dimethyladenosine transferase related protein (rRNA methylase); Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.
  
    0.814
MMP1554
Conserved hypothetical archaeal protein.
  
   
 0.707
top6B
DNA topoisomerase VI B; Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
       0.496
cdh-2
CO dehydrogenase beta subunit/acetyl-CoA synthase subunit epsilon; Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation. Belongs to the CdhB family.
       0.477
cdhA
CO dehydrogenase/acetyl-CoA synthase complex subunit alpha; Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.
       0.477
cdhB
CO dehydrogenase/acetyl-CoA synthase complex subunit beta; Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex); Belongs to the CdhC family.
       0.472
MMP0982
Conserved hypothetical protein; Putative nickel insertion protein for CO dehydrogenase, similar to cooC of Rhodospirillum rubrum; Citation: Jeon, W.B., et al. 2001. J. Biol. Chem. 276:38602-9.
       0.469
fmdE
Molybdenum containing formylmethanofuran dehydrogenase, subunit E; Citation: FEBS Lett. 1989 253:226-30; Eur. J. Biochem. 1996 242: 156-162.
  
    0.465
cdhD
CO dehydrogenase/acetyl-CoA synthase subunit delta; Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). Probably maintains the overall quaternary structure of the ACDS complex. Belongs to the CdhD family.
       0.455
Your Current Organism:
Methanococcus maripaludis S2
NCBI taxonomy Id: 267377
Other names: M. maripaludis S2, Methanococcus maripaludis LL, Methanococcus maripaludis str. S2, Methanococcus maripaludis strain S2
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.