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.
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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Neighborhood
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Co-occurrence
Co-expression
Experiments
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[Homology]
Score
rlmL23S rRNA m(2)G-2445 methyltransferase; Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. Belongs to the methyltransferase superfamily. RlmKL family. (749 aa)    
Predicted Functional Partners:
Ping_2281
PFAM: ABC transporter related; SMART: AAA ATPase; KEGG: vvy:VV1658 ABC-type transport system, ATPase component.
 
  
 0.848
Ping_2282
PFAM: glutaredoxin 2; KEGG: son:SO1852 hypothetical protein.
       0.818
Ping_2280
KEGG: pat:Patl_1429 hypothetical protein.
  
    0.816
uppS
Undecaprenyl pyrophosphate synthetase; Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di- trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
   
    0.700
Ping_0484
Multi-sensor histidine kinase with CHASE and PAS/PAC sensory domains; KEGG: neu:NE0049 sensory transduction histidine kinase; TIGRFAM: PAS sensor protein; PFAM: response regulator receiver; ATP-binding region, ATPase domain protein domain protein; histidine kinase A domain protein domain protein; CHASE domain protein; Hpt domain protein; PAS fold-3 domain protein; PAS fold domain protein; SMART: PAS domain containing protein; PAC repeat-containing protein.
     
 0.689
tgt
tRNA-guanine transglycosylase; 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 to form the [...]
  
  
 0.667
Ping_1440
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.
     
 0.633
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
  
    0.618
rimP
Hypothetical protein DUF150; Required for maturation of 30S ribosomal subunits. Belongs to the RimP family.
 
    0.603
rsmF
16S rRNA m(5)C-1407 methyltransferase; Specifically methylates the cytosine at position 1407 (m5C1407) of 16S rRNA.
  
  
 0.597
Your Current Organism:
Psychromonas ingrahamii
NCBI taxonomy Id: 357804
Other names: P. ingrahamii 37, Psychromonas ingrahamii 37, Psychromonas ingrahamii str. 37, Psychromonas ingrahamii strain 37, gas vacuolate str. 37
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.