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
CPE1320Conserved hypothetical protein; 330 aa, similar to gpu:AP001510_195 BH1020 gene product from Bacillus halodurans (391 aa); 32.7% identity in 297 aa overlap. (330 aa)    
Predicted Functional Partners:
CPE0342
Probable methylated-DNA-protein-cystein methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
      0.809
CPE1319
Probable acyltransferase; 234 aa, similar to prf:2403377A sn-glycerol-3-phosphate acyltransferase from Clostridium butyricum (234 aa); 57.1% identity in 233 aa overlap.
       0.779
CPE1318
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.
       0.773
cysE-2
169 aa, similar to sp:CYSE_HELPY SERINE ACETYLTRANSFERASE (EC 2.3.1.30) (SAT) from Helicobacter pylori (strain 26695) (171 aa); 69.1% identity in 162 aa overlap. 1 putative transmembrane region was found by PSORT; CPE1321.
       0.668
cysK-2
300 aa, similar to gp:CST130879_2 o-acetylserine sulfhydrylase from Clostridium sticklandii (304 aa); 50.8% identity in 299 aa overlap; CPE1322; cysteine synthase; Belongs to the cysteine synthase/cystathionine beta- synthase family.
       0.652
CPE2061
1171 aa, similar to gp:CPA17727_2 pyruvate ferredoxin oxidoreductase from Clostridium pasteurianum (1175 aa); 73.6% identity in 1167 aa overlap.
     
 0.479
queA
S-adenosylmethionine:tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
 
   
 0.456
CPE2480
Conserved hypothetical protein; 483 aa, similar to sp:YABN_BACSU HYPOTHETICAL 56.1 KDA PROTEIN IN MFD-DIVIC INTERGENIC REGION from Bacillus subtilis (489 aa); 47.7% identity in 484 aa overlap.
  
     0.451
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form th [...]
 
  
 0.439
Your Current Organism:
Clostridium perfringens 13
NCBI taxonomy Id: 195102
Other names: C. perfringens str. 13, Clostridium perfringens str. 13
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