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
Sare_0364PFAM: Taurine catabolism dioxygenase TauD/TfdA; KEGG: sma:SAV3636 SyrP-like protein. (326 aa)    
Predicted Functional Partners:
Sare_0363
TIGRFAM: amino acid adenylation domain; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; KEGG: mxa:MXAN_3636 non-ribosomal peptide synthetase.
  
 0.901
Sare_4562
TIGRFAM: amino acid adenylation domain; PFAM: AMP-dependent synthetase and ligase; Thioesterase; condensation domain protein; phosphopantetheine-binding; Methyltransferase type 11; Methyltransferase type 12; KEGG: mxa:MXAN_3779 non-ribosomal peptide synthetase/polyketide synthase.
  
 0.889
Sare_0362
TIGRFAM: amino acid adenylation domain; PFAM: AMP-dependent synthetase and ligase; Thioesterase; condensation domain protein; phosphopantetheine-binding; KEGG: sma:SAV3642 putative non-ribosomal peptide synthetase.
  
 0.872
Sare_2407
TIGRFAM: amino acid adenylation domain; PFAM: AMP-dependent synthetase and ligase; Thioesterase; condensation domain protein; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: sde:Sde_3725 polyketide synthase modules and related proteins-like.
 
 
 0.836
Sare_3151
Beta-ketoacyl synthase; PFAM: Thioesterase; NAD-dependent epimerase/dehydratase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; Erythronolide synthase docking; KEGG: sen:SACE_4139 type I modular polyketide synthase.
  
 0.820
Sare_4891
TIGRFAM: amino acid adenylation domain; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; KEGG: stp:Strop_4417 amino acid adenylation domain.
  
 0.760
Sare_2097
PFAM: condensation domain protein; KEGG: stp:Strop_2721 condensation domain protein.
  
 0.745
Sare_4894
TIGRFAM: amino acid adenylation domain; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; KEGG: stp:Strop_4420 amino acid adenylation domain.
  
 0.736
Sare_4890
TIGRFAM: amino acid adenylation domain; thioester reductase domain; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; 3-beta hydroxysteroid dehydrogenase/isomerase; phosphopantetheine-binding; Male sterility domain; KEGG: stp:Strop_4416 amino acid adenylation domain; Belongs to the ATP-dependent AMP-binding enzyme family.
  
 0.735
Sare_0353
TIGRFAM: amino acid adenylation domain; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; KEGG: pap:PSPA7_2859 linear gramicidin synthetase subunit D.
  
 0.725
Your Current Organism:
Salinispora arenicola
NCBI taxonomy Id: 391037
Other names: S. arenicola CNS-205, Salinispora arenicola CNS-205, Salinispora arenicola str. CNS-205, Salinispora arenicola strain CNS-205
Server load: medium (66%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.