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.
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Co-occurrence
Co-expression
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[Homology]
Score
rlmNDual-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. (386 aa)    
Predicted Functional Partners:
OOR95665.1
16S rRNA (cytosine(967)-C(5))-methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
  
  
 0.921
miaB
tRNA (N6-isopentenyl adenosine(37)-C2)-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.
 
  
 0.692
OOR96442.1
Type IV pilus biogenesis/stability protein PilW; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.691
ribD
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.
     
 0.691
OOR96318.1
YggW family oxidoreductase; 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.
  
     0.631
OOR96443.1
RNA-binding transcriptional accessory protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.563
OOR94363.1
YggS family pyridoxal phosphate enzyme; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
  
     0.509
rimO
Ribosomal protein S12 methylthiotransferase; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily.
 
  
 0.494
tgt
tRNA guanosine(34) transglycosylase Tgt; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose t [...]
   
  
 0.489
metG
methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
     
 0.485
Your Current Organism:
Haemophilus paraphrohaemolyticus
NCBI taxonomy Id: 736
Other names: ATCC 29237, CCUG 3718, CIP 102512, DSM 21451, H. paraphrohaemolyticus, NCTC 10670
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