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.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Noca_4657DnaB domain protein helicase, C-terminal domain protein; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. Belongs to the helicase family. DnaB subfamily. (824 aa)    
Predicted Functional Partners:
dnaA
Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family.
  
 
 0.916
Noca_1580
PFAM: TOPRIM domain protein; DNA primase catalytic core, N-terminal domain; SMART: Toprim sub domain protein; KEGG: mmc:Mmcs_1430 ATP-dependent exoDNAse (exonuclease V) alpha subunit - helicase superfamily I member-like protein.
 
 
 0.886
Noca_1947
KEGG: pac:PPA0957 DNA primase; TIGRFAM: DNA primase; PFAM: zinc finger, CHC2-family protein; TOPRIM domain protein; DNA primase catalytic core, N-terminal domain; SMART: Hedgehog/intein hint domain protein; Toprim sub domain protein; DNA primase DnaG, DnaB-binding.
 
 
 0.885
Noca_2250
PFAM: TOPRIM domain protein; DNA primase catalytic core, N-terminal domain; SMART: Toprim sub domain protein; KEGG: mmc:Mmcs_1430 ATP-dependent exoDNAse (exonuclease V) alpha subunit - helicase superfamily I member-like protein.
  
 
 0.871
Noca_0582
PFAM: IstB domain protein ATP-binding protein; SMART: AAA ATPase; KEGG: rha:RHA1_ro06982 possible insertion sequence ATP-binding protein.
  
 
 0.849
Noca_2757
PFAM: IstB domain protein ATP-binding protein; SMART: AAA ATPase; KEGG: rha:RHA1_ro06982 possible insertion sequence ATP-binding protein.
  
 
 0.849
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.
  
  
 0.775
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 [...]
  
  
 0.703
Noca_3810
PFAM: BRCT domain protein; Exonuclease, RNase T and DNA polymerase III; SMART: Exonuclease; KEGG: tfu:Tfu_0714 exonuclease.
  
  
 0.660
recF
DNA replication and repair protein RecF; The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
  
  
 0.636
Your Current Organism:
Nocardioides sp. JS614
NCBI taxonomy Id: 196162
Other names: N. sp. JS614
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.