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
trmIL-isoaspartyl protein carboxyl methyltransferase isolog (pimT); Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 58 (m1A58) in tRNA. Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM61 family. (282 aa)    
Predicted Functional Partners:
rnhB
Ribonuclease HII (rnhB); Endonuclease that specifically degrades the RNA of RNA-DNA hybrids; Belongs to the RNase HII family.
  
   0.950
tgtA
Queuine tRNA-ribosyltransferase (tgtA); Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs. Can also utilize guanine as substrate.
  
  
 0.881
cbiT
Cobalamin biosynthesis precorrin-8W decarboxylase (cbiT); Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
     
 0.865
rlmE
Cell division protein FtsJ; Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
   
  
 0.829
rtcA
Hypothetical protein; 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 (By similarity).
   
    0.786
rpl30
LSU ribosomal protein L30P (rpmD); Similar to SP:P14035 PID:44769 percent identity: 71.43; identified by sequence similarity; putative.
  
   0.776
MJ_1478
Conserved hypothetical protein; Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2- thiouridine (m(5)s(2)U or s(2)T) (By similarity). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is required for cell growth at high temperatures (By similarity). Belongs to the TtcA family. TtuA subfamily.
 
  
 0.776
MJ_1408
GTP-binding protein, member of GTP1/OBG-family; Similar to PID:1151233 percent identity: 30.46; identified by sequence similarity; putative; Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.
  
    0.731
rps8e
SSU ribosomal protein S8E; Similar to SP:P49402 percent identity: 50.00; identified by sequence similarity; putative.
  
    0.723
trmG10
Conserved hypothetical protein; Catalyzes the adenosylmethionine-dependent methylation of the exocyclic amino group (N(2)) of guanosine at position 10 of various tRNAs. Acts via a two-step process that leads to the formation of either N(2)-monomethyl (m(2)G) or N(2)-dimethylguanosine (m(2)(2)G) (By similarity); Belongs to the methyltransferase superfamily. Trm-G10 family.
   
  
 0.712
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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