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
rlmNRadical SAM domain protein; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. (342 aa)    
Predicted Functional Partners:
Sfum_0150
Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
  
  
 0.964
Sfum_4058
PFAM: histone deacetylase superfamily; KEGG: sat:SYN_02870 histone deacetylase domain protein.
       0.777
miaB
tRNA-i(6)A37 thiotransferase enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
 
  
 0.767
rimO
MiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily.
 
  
 0.754
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
  
    0.702
Sfum_0166
RNA modification enzyme, MiaB family; KEGG: sat:SYN_00797 tRNA 2-methylthioadenosine synthase -like protein; TIGRFAM: RNA modification enzyme, MiaB family; MiaB-like tRNA modifying enzyme; PFAM: Radical SAM domain protein; Protein of unknown function UPF0004-like; SMART: Elongator protein 3/MiaB/NifB.
 
  
 0.666
Sfum_4054
PFAM: TPR repeat-containing protein; Sporulation domain protein; Tetratricopeptide TPR_4; Tetratricopeptide TPR_2 repeat protein; SMART: Tetratricopeptide domain protein; KEGG: sat:SYN_01414 tetratricopeptide repeat family protein.
  
    0.652
Sfum_1360
Coproporphyrinogen III oxidase, anaerobic; 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.
 
   
 0.633
hisG
ATP phosphoribosyltransferase (homohexameric); Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
       0.626
hisI
phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
       0.626
Your Current Organism:
Syntrophobacter fumaroxidans
NCBI taxonomy Id: 335543
Other names: S. fumaroxidans MPOB, Syntrophobacter fumaroxidans DSM 10017, Syntrophobacter fumaroxidans MPOB, Syntrophobacter fumaroxidans str. MPOB, Syntrophobacter fumaroxidans strain MPOB, Syntrophobacter sp. DSM 10017, syntrophic propionate-oxidizing bacterium DSM 10017
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