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
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[Homology]
Score
SMB91343.1Radical SAM superfamily enzyme YgiQ, UPF0313 family; InterPro IPR006638:IPR006158:IPR007197; COGs: COG1032 Fe-S oxidoreductase; KEGG: mta:Moth_0197 radical SAM family protein; SPTR: Radical SAM; SMART: Elongator protein 3/MiaB/NifB; PFAM: Radical SAM domain protein; cobalamin B12-binding domain protein. (603 aa)    
Predicted Functional Partners:
SMB92770.1
InterProIPR002078:IPR000014:IPR003593:IPR004096:IPR 013656:IPR002197:IPR001901:IPR020441; COGs: COG3829 Transcriptional regulator containing PAS AAA-type ATPase and DNA-binding domains; KEGG: tte:TTE1710 transcriptional regulator; SPTR: NtrC family Transcriptional regulator, ATPase domain protein; SMART: AAA ATPase; PAS domain containing protein; PFAM: sigma-54 factor interaction domain-containing protein; 4-vinyl reductase 4VR; PAS fold-4 domain protein; helix-turn-helix Fis-type.
  
 
 0.829
SMB92708.1
Haem-NO-binding; InterPro IPR011644; KEGG: cwo:Cwoe_5547 heme NO binding domain protein; SPTR: Heme NO binding domain protein; PFAM: Heme NO binding domain protein.
  
 
 0.811
SMB92584.1
XTP/dITP diphosphohydrolase; 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.
      0.583
thiI
Thiamine biosynthesis protein ThiI; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
       0.547
SMB92909.1
Oxygen-independent coproporphyrinogen-3 oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family.
  
  
 0.428
SMB91349.1
Cysteine desulfurase; InterPro IPR000192:IPR016454; COGs: COG1104 Cysteine sulfinate desulfinase/cysteine desulfurase; KEGG: mta:Moth_0199 aminotransferase, class V; SPTR: Aminotransferase, class V; PFAM: aminotransferase class V.
       0.422
SMB93801.1
Peptidase family M1; InterPro IPR014782; KEGG: mta:Moth_0738 peptidase M1, membrane alanine aminopeptidase; SPTR: Peptidase M1, membrane alanine aminopeptidase; PFAM: Peptidase M1 membrane alanine aminopeptidase.
  
     0.415
Your Current Organism:
Thermanaeromonas toyohensis
NCBI taxonomy Id: 698762
Other names: T. toyohensis ToBE, Thermanaeromonas toyohensis DSM 14490, Thermanaeromonas toyohensis ToBE, Thermanaeromonas toyohensis str. ToBE, Thermanaeromonas toyohensis strain ToBE, Thermoanaerobacter sp. ToBE
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