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
rtcBProtein of unknown function UPF0027; GTP-dependent RNA ligase that is involved in tRNA splicing and RNA repair. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends; Belongs to the RtcB family. (480 aa)    
Predicted Functional Partners:
MMP0647
ATP/GTP-binding site motif A (P-loop):Protein of unknown function DUF101; Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently.
 
 0.967
rtcA
RNA 3'-terminal phosphate cyclase; Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
 
  
 0.933
flpA-2
Fibrillarin; Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA; Belongs to the methyltransferase superfamily. Fibrillarin family.
   
 0.709
asd
Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.
  
    0.709
MMP0457
Probable ATP dependent RNA helicase; Citation: Mol. Cell 2001; 8:251-62. Nucleic Acids Res. 1999; 27:3811-20. Prog. Nucleic Acid Res. Biol. 2002; 72:307-31, PNAS (2001) 98:; Belongs to the DEAD box helicase family.
   
 0.697
prf1
Peptide chain release factor aRF, subunit 1; Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
  
    0.651
tgtA
tRNA-guanine(15) transglycosylase; Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs; Belongs to the archaeosine tRNA-ribosyltransferase family.
  
  
 0.598
aIF-1A
Translation initiation factor 1A (aIF-1A); Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
     
 0.546
MMP1393
Conserved hypothetical protein.
       0.545
MMP1036
Band 7 protein:Stomatin.
  
 
 0.537
Your Current Organism:
Methanococcus maripaludis S2
NCBI taxonomy Id: 267377
Other names: M. maripaludis S2, Methanococcus maripaludis LL, Methanococcus maripaludis str. S2, Methanococcus maripaludis strain S2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.