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
KXA30444.1Hypothetical protein; KEGG: tsi:TSIB_1797 0.00015 V-type ATP synthase subunit I K02123; Psort location: Cytoplasmic, score: 7.50. (269 aa)    
Predicted Functional Partners:
ruvC
Crossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
       0.696
ruvA
Holliday junction DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
       0.696
ruvB
Holliday junction DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
       0.695
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).
       0.673
tgt
tRNA-guanine transglycosylase; 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 the [...]
       0.672
asnA
Aspartate--ammonia ligase; KEGG: fnu:FN0776 8.9e-105 asparagine synthetase AsnA K01914; Psort location: Cytoplasmic, score: 10.00.
       0.655
KXA30448.1
SpoIID/LytB domain protein; KEGG: bqy:MUS_3906 4.3e-29 lytC1; N-acetylmuramoyl-L-alanine amidase; Psort location: Cellwall, score: 8.75.
       0.629
KXA30442.1
Hypothetical protein; Psort location: Cytoplasmic, score: 7.50.
       0.556
yajC
Preprotein translocase, YajC subunit; KEGG: apb:SAR116_0407 1.4e-10 YajC K03210.
       0.520
KXA30452.1
rSAM-modified six-cysteine peptide; Psort location: Extracellular, score: 8.91.
       0.445
Your Current Organism:
Peptoniphilus harei
NCBI taxonomy Id: 54005
Other names: ATCC BAA-601, CCUG 38491, CIP 105323, DSM 10020, NCTC 13076, P. harei, Peptostreptococcus harei, Schleiferella harei
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.