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
Lbys_1323COGs: COG2935 Putative arginyl-tRNA:protein arginylyltransferase; InterPro IPR007472; KEGG: chu:CHU_2143 arginyl-tRNA:protein arginylyltransferase; PFAM: Arginine-tRNA-protein transferase domain protein; SPTR: Arginyl-tRNA:protein arginylyltransferase; PFAM: Arginine-tRNA-protein transferase, C terminus. (354 aa)    
Predicted Functional Partners:
nuoB
NADH dehydrogenase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
       0.773
nuoA
NADH dehydrogenase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family.
       0.773
Lbys_1911
Guanine-specific ribonuclease N1 and T1; COGs: COG4290 Guanyl-specific ribonuclease Sa; InterPro IPR000026; KEGG: tpr:Tpau_0946 guanine-specific ribonuclease N1 and T1; PFAM: guanine-specific ribonuclease N1 and T1; SPTR: Probable guanyl-specific ribonuclease; PFAM: ribonuclease.
  
     0.508
Lbys_3485
OmpA/MotB domain protein; COGs: COG2885 Outer membrane protein and related peptidoglycan-associated (lipo)protein; InterPro IPR006664:IPR006665:IPR011659; KEGG: sli:Slin_3584 OmpA/MotB domain protein; PFAM: OmpA/MotB domain protein; WD40-like beta Propeller containing protein; SPTR: OmpA/MotB domain protein; PFAM: WD40-like Beta Propeller Repeat; OmpA family.
  
     0.486
Lbys_1921
Conserved repeat domain protein; InterPro IPR000601:IPR019775:IPR001434; KEGG: sli:Slin_3586 conserved repeat domain protein; PFAM: protein of unknown function DUF11; SPTR: Conserved repeat domain protein; TIGRFAM: conserved repeat domain protein; TIGRFAM: conserved repeat domain.
  
     0.448
Lbys_2032
InterPro IPR008910; KEGG: sli:Slin_4747 TM helix repeat-containing protein; PFAM: Conserved TM helix repeat-containing protein; SPTR: Conserved TM helix repeat-containing protein; PFAM: Mechanosensitive ion channel; Conserved TM helix.
  
 
   0.419
Lbys_2991
Hypothetical protein; KEGG: cpi:Cpin_2776 fibronectin type III domain protein; SPTR: Fibronectin type III domain protein; TIGRFAM: Bacteroides forsythus 147-residue repeat.
  
     0.417
Your Current Organism:
Leadbetterella byssophila
NCBI taxonomy Id: 649349
Other names: L. byssophila DSM 17132, Leadbetterella byssophila 4M15, Leadbetterella byssophila DSM 17132, Leadbetterella byssophila str. DSM 17132, Leadbetterella byssophila strain DSM 17132
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