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
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
mjaIVMPModification methylase, type II R/M system; This methylase recognizes the double-stranded sequence GTNNAC, causes specific methylation on ? on both strands, and protects the DNA from cleavage by the MjaIV endonuclease. (298 aa)    
Predicted Functional Partners:
rqcH
Conserved hypothetical protein; Probably part of the ribosome quality control system (RQC). May mediate the addition of alanine residues (Ala tailing) to incompletely synthesized nascent chains from stalled ribosomes, leading to their degradation; Belongs to the NEMF family.
  
    0.897
map
Methionyl aminopeptidase (map); Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.
       0.773
MJ_1531
Type I restriction-modification enzyme, S subunit, putative; Similar to GB:X17591 PID:40467 percent identity: 37.84; identified by sequence similarity; putative; To M.jannaschii MJ0130 and MJ1218.
 
  
 0.532
MJ_0132
Type I restriction-modification enzyme 2, M subunit; Similar to GB:L25415 PID:496158 percent identity: 39.36; identified by sequence similarity; putative; Belongs to the N4/N6-methyltransferase family.
  
  
 0.511
MJ_1220
Type I restriction-modification enzyme 1, M subunit; Similar to GB:L25415 PID:496158 percent identity: 32.85; identified by sequence similarity; putative.
  
  
 0.511
MJ_0130
Type I restriction-modification enzyme 2, S subunit; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a mai [...]
 
  
 0.490
MJ_1218
Type I restriction-modification enzyme 1, S subunit; Identified by sequence similarity; putative.
 
  
 0.489
MJ_1330
Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 54.47; identified by sequence similarity; putative.
       0.479
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
Server load: low (16%) [HD]