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
EHA62482.1TIGRFAM: Mutator MutT; PFAM: NUDIX hydrolase domain; HhH-GPD domain; Endonuclease III-like, iron-sulphur cluster loop motif; KEGG: pmf:P9303_01721 adenine glycosylase; SMART: HhH-GPD domain; Endonuclease III-like, iron-sulphur cluster loop motif. (395 aa)    
Predicted Functional Partners:
EHA64252.1
Exodeoxyribonuclease III; TIGRFAM: AP endonuclease, family 1; Exodeoxyribonuclease III xth; KEGG: pmf:P9303_06981 exodeoxyribonuclease III; PFAM: Endonuclease/exonuclease/phosphatase.
    
 0.965
EHA59101.1
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 [...]
    
 
 0.792
EHA62483.1
KEGG: rpb:RPB_0923 resolvase-like protein; PFAM: Resolvase, N-terminal; SMART: Resolvase, N-terminal.
     
 0.773
nth
Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate.
  
 
 0.630
EHA62481.1
Fructokinase; KEGG: pmt:PMT0136 putative carbohydrate kinase; PFAM: Carbohydrate/purine kinase.
       0.609
EHA62421.1
KEGG: pmc:P9515_13871 hypothetical protein; PFAM: Dual specificity phosphatase, catalytic domain; SMART: Dual specificity phosphatase, subgroup, catalytic domain.
  
   
 0.603
sfsA
TIGRFAM: Sugar fermentation stimulation protein; HAMAP: Sugar fermentation stimulation protein; KEGG: pmf:P9303_24781 sugar fermentation stimulation protein A; PFAM: Sugar fermentation stimulation protein; Belongs to the SfsA family.
 
    0.537
EHA62484.1
PFAM: Protein of unknown function DUF411; KEGG: oan:Oant_2533 hypothetical protein.
       0.522
ribBA
3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family.
    
   0.435
EHA60114.1
Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family.
  
     0.429
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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