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
AMC10514.123S rRNA pseudouridine synthase F; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the pseudouridine synthase RsuA family. (267 aa)    
Predicted Functional Partners:
der
Ribosome-associated GTPase EngA; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
 
  
 0.716
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 t [...]
 
 
 0.708
cmk
Cytidylate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.705
AMC11263.1
Exodeoxyribonuclease III; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.647
AMC12194.1
Permease; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.559
AMC10516.1
Permease; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.552
accA
acetyl-CoA carboxyl transferase; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
       0.435
AMC10513.1
Integrase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.433
nnrD
Carbohydrate kinase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epim [...]
       0.429
Your Current Organism:
Lutibacter profundi
NCBI taxonomy Id: 1622118
Other names: DSM 100437, JCM 30586, L. profundi, Lutibacter profundi Le Moine Bauer et al. 2016, Lutibacter sp. LP1, strain LP1
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