STRINGSTRING
rnt protein (Pseudomonas oleovorans) - STRING interaction network
"rnt" - Ribonuclease T in Pseudomonas oleovorans
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
rntRibonuclease T; Trims short 3’ overhangs of a variety of RNA species, leaving a one or two nucleotide 3’ overhang. Responsible for the end-turnover of tRNA- specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis (224 aa)    
Predicted Functional Partners:
rnd
Ribonuclease D; Exonuclease involved in the 3’ processing of various precursor tRNAs. Initiates hydrolysis at the 3’-terminus of an RNA molecule and releases 5’-mononucleotides; Belongs to the RNase D family (377 aa)
 
  0.924
rph
Ribonuclease PH; Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates (239 aa)
   
 
  0.917
pyrC
Dihydroorotase; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate (348 aa)
   
   
  0.917
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (931 aa)
   
 
  0.890
JNHE01000024_gene2490
Beta sliding clamp; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3’-5’ exonuclease proofreading activity. The beta chain is required for initiation of replication as [...] (367 aa)
     
  0.840
JNHE01000036_gene4300
annotation not available (984 aa)
   
  0.828
JNHE01000019_gene4153
annotation not available (1176 aa)
   
  0.828
rnpA
Ribonuclease P protein component; RNaseP catalyzes the removal of the 5’-leader sequence from pre-tRNA to produce the mature 5’-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5’-leader sequence and broadening the substrate specificity of the ribozyme (84 aa)
   
 
    0.827
dnaX
DNA polymerase III subunit gamma/tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity (678 aa)
     
  0.825
JNHE01000003_gene1852
annotation not available (999 aa)
       
  0.822
Your Current Organism:
Pseudomonas oleovorans
NCBI taxonomy Id: 301
Other names: ATCC 8062, CCUG 2087, CFBP 5589, CIP 59.11, IFO 13583, JCM 11598, LMG 2229, NBRC 13583, NCIMB 6576, NCTC 10692, NRRL B-778, P. oleovorans, Pseudomonas oleovorans, Pseudomonas sp. MGY01
Server load: low (12%) [HD]