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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
EIJ34585.1PFAM: Glutaredoxin; TIGRFAM: Glutaredoxin, GrxC family; COGs: COG0695 Glutaredoxin and related protein; InterPro IPR002109:IPR011900; KEGG: rcp:RCAP_rcc00198 glutaredoxin; PFAM: Glutaredoxin; SPTR: Glutaredoxin 3; TIGRFAM: Glutaredoxin, GrxC. (87 aa)    
Predicted Functional Partners:
EIJ34584.1
PFAM: Preprotein translocase subunit SecB; TIGRFAM: protein-export chaperone SecB; COGs: COG1952 Preprotein translocase subunit SecB; HAMAP: Bacterial protein export chaperone SecB; InterPro IPR003708; KEGG: shm:Shewmr7_0045 preprotein translocase subunit SecB; PFAM: Bacterial protein export chaperone SecB; SPTR: Protein-export protein secB; TIGRFAM: Bacterial protein export chaperone SecB.
  
  
 0.970
EIJ34586.1
PFAM: Rhodanese-like domain; COGs: COG0607 Rhodanese-related sulfurtransferase; InterPro IPR001763; KEGG: tkm:TK90_2023 rhodanese; PFAM: Rhodanese-like; SMART: Rhodanese-like; SPTR: Rhodanese domain protein.
  
    0.933
EIJ35309.1
Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
  
 0.909
EIJ34582.1
PFAM: Prokaryotic glutathione synthetase, N-terminal domain; Prokaryotic glutathione synthetase, ATP-grasp domain; TIGRFAM: glutathione synthetase, prokaryotic; COGs: COG0189 Glutathione synthase/Ribosomal protein S6 modification enzyme (glutaminyl transferase); HAMAP: Glutathione synthetase, prokaryotic; InterPro IPR004215:IPR004218:IPR006284; KEGG: tgr:Tgr7_2905 glutathione synthetase; PFAM: Prokaryotic glutathione synthetase, ATP-binding; Prokaryotic glutathione synthetase, N-terminal; SPTR: Glutathione synthetase; TIGRFAM: Glutathione synthetase, prokaryotic.
 
  
 0.843
EIJ34583.1
PFAM: NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; COGs: COG0240 Glycerol-3-phosphate dehydrogenase; HAMAP: Glycerol-3-phosphate dehydrogenase [NAD(P)+]; InterPro IPR011128:IPR006109; KEGG: tgr:Tgr7_3281 NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; PFAM: NAD-dependent glycerol-3-phosphate dehydrogenase, C-terminal; NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal; SPTR: Glycerol-3-phosphate dehydrogenase [NAD(P)+].
  
  
 0.820
EIJ33537.1
PFAM: GTP cyclohydrolase II; 3,4-dihydroxy-2-butanone 4-phosphate synthase; TIGRFAM: 3,4-dihydroxy-2-butanone 4-phosphate synthase; COGs: COG0108 3 4-dihydroxy-2-butanone 4-phosphate synthase; HAMAP: 3,4-dihydroxy-2-butanone 4-phosphate synthase; InterPro IPR000422:IPR000926; KEGG: tgr:Tgr7_1561 3,4-dihydroxy-2-butanone 4-phosphate synthase; PFAM: DHBP synthase RibB; GTP cyclohydrolase II; SPTR: 3,4-dihydroxy-2-butanone 4-phosphate synthase; TIGRFAM: DHBP synthase RibB.
    
  0.803
atpF
ATP synthase subunit b; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family.
  
    0.802
EIJ36529.1
Methionine synthase (B12-dependent); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
    
 0.785
EIJ34264.1
Adenylate/guanylate cyclase with Chase sensor; PFAM: Adenylate and Guanylate cyclase catalytic domain; CHASE2 domain; COGs: COG2114 Adenylate cyclase family 3 (some protein contain HAMP domain); InterPro IPR001054:IPR007890; KEGG: bge:BC1002_5478 adenylate/guanylate cyclase with Chase sensor; PFAM: Adenylyl cyclase class-3/4/guanylyl cyclase; CHASE2; SMART: Adenylyl cyclase class-3/4/guanylyl cyclase; SPTR: Adenylate/guanylate cyclase with Chase sensor.
     
  0.726
EIJ34311.1
PFAM: Adenylate and Guanylate cyclase catalytic domain; CHASE2 domain; COGs: COG2114 Adenylate cyclase family 3 (some protein contain HAMP domain); InterPro IPR001054:IPR007890; KEGG: cti:RALTA_B1920 adenylate cyclase with chase2 domain; PFAM: Adenylyl cyclase class-3/4/guanylyl cyclase; CHASE2; SMART: Adenylyl cyclase class-3/4/guanylyl cyclase; SPTR: Putative Adenylate cyclase with Chase2 domain.
     
  0.726
Your Current Organism:
Thiothrix nivea
NCBI taxonomy Id: 870187
Other names: T. nivea DSM 5205, Thiothrix nivea DSM 5205, Thiothrix nivea JP2, Thiothrix nivea str. DSM 5205, Thiothrix nivea strain DSM 5205
Server load: low (14%) [HD]