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
rlmN23S rRNA m(2)A-2503 methyltransferase; 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. (356 aa)    
Predicted Functional Partners:
Mmc1_0052
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.
 
   
 0.738
rimO
SSU ribosomal protein S12P methylthiotransferase; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily.
 
  
 0.723
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.
 
  
 0.722
ndk
Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family.
  
    0.704
Mmc1_3469
PFAM: Fmu (Sun) domain protein; KEGG: mfa:Mfla_0208 Fmu (Sun); Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
 
  
 0.661
nusB
NusB antitermination factor; Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
  
  
 0.648
Mmc1_0976
MiaB-like tRNA modifying enzyme; KEGG: mag:amb0214 2-methylthioadenine synthetase; 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.
 
  
 0.642
Mmc1_3668
16S rRNA m(5)C-967 methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
  
  
 0.617
efp
Translation elongation factor P (EF-P); Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
  
  
 0.582
Mmc1_0168
Diaminohydroxyphosphoribosylaminopyrimidine deaminase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
     
 0.557
Your Current Organism:
Magnetococcus marinus
NCBI taxonomy Id: 156889
Other names: M. marinus MC-1, Magnetococcus marinus MC-1, Magnetococcus marinus str. MC-1, Magnetococcus marinus strain MC-1, Magnetococcus sp. MC-1
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