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
mcsBATP:guanido phosphotransferase; Catalyzes the specific phosphorylation of arginine residues in proteins. (356 aa)    
Predicted Functional Partners:
AEG58558.1
PFAM: UvrB/UvrC protein; KEGG: drm:Dred_0178 UvrB/UvrC protein.
 
 
 0.999
AEG58557.1
PFAM: Firmicute transcriptional repressor of class III stress genes; KEGG: drm:Dred_0177 Firmicute transcriptional repressor of class III stress genes; Belongs to the CtsR family.
 
  
 0.984
AEG58560.1
KEGG: drm:Dred_0180 ATPase; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; Belongs to the ClpA/ClpB family.
 
 
 0.963
radA
DNA repair protein RadA; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
  
    0.816
clpB
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.
  
 
 0.748
AEG61902.1
KEGG: drm:Dred_3164 protein tyrosine phosphatase; PFAM: Protein-tyrosine phosphatase, low molecular weight; SMART: Protein-tyrosine phosphatase, low molecular weight.
  
  
 0.725
disA
DNA integrity scanning, DisA, linker region; Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP acts as a signaling molecule that couples DNA integrity with progression of sporulation. The rise in c-di-AMP level generated by DisA while scanning the chromosome, operates as a positive signal that advances sporulation; upon encountering a lesion, the DisA focus arrests at the damaged site and halts c-di-AMP synthesis.
  
    0.656
AEG59628.1
KEGG: drm:Dred_2312 pyruvate kinase; TIGRFAM: pyruvate kinase; PFAM: Pyruvate kinase barrel; Pyruvate kinase alpha/beta; PEP-utilising protein mobile region; Belongs to the pyruvate kinase family.
   
 
 0.531
AEG58565.1
KEGG: drm:Dred_0186 PilT domain-containing protein; PFAM: PilT protein domain protein; deoxyribonuclease/rho motif-related TRAM; SMART: Nucleotide binding protein PINc.
 
    0.530
hrcA
Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
   
  
 0.519
Your Current Organism:
Desulfotomaculum ruminis
NCBI taxonomy Id: 696281
Other names: D. ruminis DSM 2154, Desulfotomaculum ruminis ATCC 23193, Desulfotomaculum ruminis DL, Desulfotomaculum ruminis DSM 2154, Desulfotomaculum ruminis str. DSM 2154, Desulfotomaculum ruminis strain DSM 2154
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.