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
hemN_2Oxygen-independent coproporphyrinogen-III oxidase 1; 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. (387 aa)    
Predicted Functional Partners:
rdgB
dITP/XTP pyrophosphatase; 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.
 
    0.890
rlmN
Dual-specificity RNA methyltransferase RlmN; 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.
 
   
 0.731
SBO12124.1
Hypothetical protein.
       0.672
SBO12128.1
Hypothetical protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
 
     0.671
miaB
(Dimethylallyl)adenosine tRNA methylthiotransferase 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.
 
   
 0.656
proC
Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
 
     0.637
SBO12125.1
Hypothetical protein; Belongs to the UPF0235 family.
       0.624
SBO12126.1
YGGT family protein.
       0.624
yhdE
Maf-like protein YhdE; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
 
   
 0.515
dosC_3
Diguanylate cyclase DosC.
  
  
 0.485
Your Current Organism:
Vibrio mediterranei
NCBI taxonomy Id: 689
Other names: ATCC 43341, ATCC BAA-91 [[Vibrio shilonii]], ATCC:BAA:91 [[Vibrio shilonii]], CAIM 316, CCUG 19040, CECT 621, CIP 103203, CIP 107136 [[Vibrio shilonii]], DSM 13774 [[Vibrio shilonii]], DSM 19502, IFO 15635, LMG 11258, LMG 19703 [[Vibrio shilonii]], LMG:11258, LMG:19703 [[Vibrio shilonii]], NBRC 15635, NCTC 11946, V. mediterranei, Vibrio mediterraneus, Vibrio shiloi, Vibrio shiloi (sic) Kushmaro et al. 2001, Vibrio shilonii, Vibrio shilonii corrig. Kushmaro et al. 2001, strain 50, strain AK1 [[Vibrio shilonii]]
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.