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.
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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
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Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
MJ_1554Conserved hypothetical protein; Similar to GB:AE000782 percent identity: 42.23; identified by sequence similarity; putative. (622 aa)    
Predicted Functional Partners:
fen
DNA repair protein RAD2 (rad2); Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) [...]
   
 0.948
pcn
Proliferating-cell nuclear antigen (pol30); Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication. Belongs to the PCNA family.
    
 0.944
aspS
aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
  
 0.931
pol
DNA polymerase B1; Similar to GB:D29671 PID:473967 PID:1620911 percent identity: 46.87; identified by sequence similarity; putative; Belongs to the DNA polymerase type-B family.
   
 0.929
topA
DNA topoisomerase I (topA) {Bacillus subtilis; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken stra [...]
    
 0.927
rpl1
LSU ribosomal protein L1P (rplA); Probably involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.
    
 0.913
rpa
Replication factor A related protein; Probably plays an essential for replication of the chromosome, DNA recombination and repair (By similarity). Binds approximately 20 nucleotides.
    
 0.882
MJ_0942
ATP-dependent DNA helicase DinG, putative (dinG); Similar to GP:1736447 percent identity: 30.88; identified by sequence similarity; putative.
   
 0.881
top6A
DNA topoisomerase VI, subunit A (top6A); Relaxes both positive and negative superturns and exhibits a strong decatenase activity; Belongs to the TOP6A family.
 
 
 
 0.876
MJ_1505
ATP dependent RNA helicase, putative; Similar to GB:Z47047 SP:P40562 PID:557851 PID:763347 percent identity: 31.59; identified by sequence similarity; putative.
    
 0.873
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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