STRINGSTRING
STRING protein interaction network
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
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[Homology]
Score
guaAAGMP synthase, small subunit; Catalyzes the synthesis of GMP from XMP. (189 aa)    
Predicted Functional Partners:
Msed_0200
PFAM: GMP synthase domain protein.
  
 0.998
Msed_2226
dITPase; 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.
 
 
 0.946
purA
Adenylosuccinate synthetase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.
 
  
 0.844
map
Methionine aminopeptidase, type II; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.
  
    0.795
gatB
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
  
 
 0.758
Msed_0018
TIGRFAM: adenylosuccinate lyase; PFAM: fumarate lyase; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
 
  
 0.745
rpl11
LSU ribosomal protein L11P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors; Belongs to the universal ribosomal protein uL11 family.
 
    0.737
argS
TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 0.737
Msed_1877
TIGRFAM: chorismate mutase; PFAM: Chorismate mutase; Prephenate dehydrogenase; NADP oxidoreductase, coenzyme F420-dependent; Shikimate/quinate 5-dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase, NAD-binding.
  
    0.706
purL
Phosphoribosylformylglycinamidine synthase subunit II; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to [...]
  
  
 0.685
Your Current Organism:
Metallosphaera sedula
NCBI taxonomy Id: 399549
Other names: M. sedula DSM 5348, Metallosphaera sedula DSM 5348, Metallosphaera sedula IFO 15509, Metallosphaera sedula JCM 9185, Metallosphaera sedula NBRC 15509, Metallosphaera sedula str. DSM 5348, Metallosphaera sedula strain DSM 5348
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