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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
nrdRATP-cone domain protein; Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR- boxes; Belongs to the NrdR family. (154 aa)    
Predicted Functional Partners:
Mvan_3426
KEGG: mmc:Mmcs_2496 cobaltochelatase, CobN subunit; TIGRFAM: cobaltochelatase, CobN subunit; PFAM: CobN/magnesium chelatase.
      
 0.811
recD
DNA helicase/exodeoxyribonuclease V, alpha subunit; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recomb [...]
      
 0.797
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.
 
   
 0.726
Mvan_2690
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
  
  
 0.695
Mvan_2442
PFAM: Peptidoglycan-binding LysM; KEGG: mmc:Mmcs_2169 peptidoglycan-binding LysM.
  
    0.665
Mvan_2303
cob(I)yrinic acid a,c-diamide adenosyltransferase; TIGRFAM: cob(I)alamin adenosyltransferase; PFAM: ATP:corrinoid adenosyltransferase BtuR/CobO/CobP; KEGG: mmc:Mmcs_2072 cob(I)alamin adenosyltransferase.
     
 0.648
Mvan_0378
KEGG: tfu:Tfu_0310 precorrin-6x reductase CbiJ/CobK; TIGRFAM: precorrin-6x reductase; PFAM: Precorrin-6x reductase CbiJ/CobK.
      
 0.642
Mvan_3434
KEGG: mpa:MAP1817c precorrin-6Y C5,15-methyltransferase / precorrin-8W decarboxylase; TIGRFAM: precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; PFAM: Uroporphyrin-III C/tetrapyrrole (Corrin/Porphyrin) methyltransferase.
     
 0.639
Mvan_2060
Ribonucleoside-diphosphate reductase class Ib beta subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides; Belongs to the ribonucleoside diphosphate reductase small chain family.
     
 0.577
Mvan_2040
Ribonucleoside-diphosphate reductase class Ib glutaredoxin subunit; TIGRFAM: Glutaredoxin-like protein NrdH; PFAM: glutaredoxin; KEGG: mmc:Mmcs_1815 glutaredoxin-like protein NrdH.
  
  
 0.548
Your Current Organism:
Mycolicibacterium vanbaalenii
NCBI taxonomy Id: 350058
Other names: M. vanbaalenii PYR-1, Mycobacterium sp. PYR-1, Mycobacterium vanbaalenii DSM 7251, Mycobacterium vanbaalenii PYR-1, Mycolicibacterium vanbaalenii DSM 7251, Mycolicibacterium vanbaalenii PYR-1
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