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
dinBDNA-directed DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. (357 aa)    
Predicted Functional Partners:
Mmc1_0002
DNA polymerase III, beta subunit; 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 [...]
  
 0.963
Mmc1_3538
PFAM: Alcohol dehydrogenase, zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KEGG: ava:Ava_3336 zinc-containing alcohol dehydrogenase superfamily.
  
    0.759
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
  
 0.750
recA
RecA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
  
 0.658
Mmc1_3229
KEGG: gme:Gmet_1215 DNA polymerase III, alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP C-terminal domain protein; nucleic acid binding, OB-fold, tRNA/helicase-type; SMART: phosphoesterase PHP domain protein.
 
  
 0.628
Mmc1_2126
Peptidylprolyl isomerase, FKBP-type; PFAM: FKBP-type peptidyl-prolyl isomerase domain protein; peptidylprolyl isomerase, FKBP-type; KEGG: par:Psyc_2090 possible peptidyl-prolyl isomerase.
    
 
 0.604
lexA
SOS-response transcriptional repressor, LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
 
 
 0.572
Mmc1_2541
KEGG: pfo:Pfl_3001 DNA topoisomerase III; TIGRFAM: DNA topoisomerase III; PFAM: TOPRIM domain protein; DNA topoisomerase, type IA, central domain protein; DNA topoisomerase, type IA, Zn finger domain protein; SMART: DNA topoisomerase I, ATP-binding; DNA topoisomerase I, DNA-binding; Toprim sub domain protein.
  
 
 0.541
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 [...]
  
 
 0.541
Mmc1_1500
Phage repressor protein, Serine peptidase, MEROPS family S24; PFAM: helix-turn-helix domain protein; peptidase S24, S26A and S26B; KEGG: psb:Psyr_2812 helix-turn-helix motif:peptidase S24, S26A and S26B.
  
 
 0.532
Your Current Organism:
Magnetococcus marinus
NCBI taxonomy Id: 156889
Other names: M. marinus MC-1, Magnetococcus marinus MC-1, Magnetococcus marinus str. MC-1, Magnetococcus marinus strain MC-1, Magnetococcus sp. MC-1
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