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
rfcAReplication factor C, small subunit; Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA; Belongs to the activator 1 small subunits family. RfcS subfamily. (315 aa)    
Predicted Functional Partners:
pcnA
Proliferating cell nuclear antigen, PCNA; 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.
 
 0.995
dnaB
DNA polymerase family B; Citation: J Bact 176:6402-6403 1994. Genes. Genet. Syst. 1998; 73: 323-336.
  
 0.988
rpa
Replication protein A; Citation: PNAS (1998) 95: 14634-14639, Annu. Rev. Biochem. (1997) 66: 61-91.
  
 0.941
MMP0122
Conserved hypothetical protein.
  
 0.940
DP1
DNA polymerase, archaeal type II, small subunit; Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase; Belongs to the DNA polymerase delta/II small subunit family.
   
 0.937
lig
ATP-dependent DNA ligase; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
  
 0.931
topA
DNA topoisomerase I; 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 strand, thus removing DNA supe [...]
 
 0.923
fen-1
Flap endonuclease; 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) pathway. Act [...]
  
 0.902
MMP0470
MCM family related protein; Citation: Nucleic Acids Res. 1992; 20: 5571-7. Molec. Microbiol. 1998; 29: 955-961; Belongs to the MCM family.
 
 
 0.893
ppsA
Phosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family.
  
  
 0.889
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.