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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.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AFZ72505.1Nicotinic acid phosphoribosyltransferase; PFAM: Quinolinate phosphoribosyl transferase, C-terminal domain. (401 aa)    
Predicted Functional Partners:
nadC
Nicotinate-nucleotide pyrophosphorylase; Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family.
   
 0.959
AFZ72011.1
PFAM: Cytidylyltransferase; TIGRFAM: nicotinamide-nucleotide adenylyltransferase; cytidyltransferase-related domain.
    
 0.955
AFZ73219.1
PFAM: Competence-damaged protein; TIGRFAM: competence/damage-inducible protein CinA C-terminal domain.
  
 
 0.944
surE
5'/3'-nucleotidase SurE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family.
     
 0.905
surE-2
5'/3'-nucleotidase SurE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family.
     
 0.905
AFZ72503.1
Nicotinamidase-like amidase; PFAM: Isochorismatase family.
 
  
 0.842
nadE
NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
 
  
 0.832
AFZ73587.1
Hypothetical protein.
  
    0.732
AFZ72504.1
Hypothetical protein.
       0.653
aspC
aspartyl-tRNA synthetase, archaeal type; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
  
  
 0.645
Your Current Organism:
Natronobacterium gregoryi
NCBI taxonomy Id: 797304
Other names: N. gregoryi SP2, Natronobacterium gregoryi ATCC 43098, Natronobacterium gregoryi JCM 8860, Natronobacterium gregoryi NCIMB 2189, Natronobacterium gregoryi SP2, Natronobacterium gregoryi str. SP2, Natronobacterium gregoryi strain SP2
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