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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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from curated databases
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Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
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[Homology]
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ADW19431.1COGs: COG0721 Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit; InterPro IPR003837; KEGG: gsu:GSU3383 glutamyl-tRNA(Gln) amidotransferase, C subunit; PFAM: Glu-tRNAGln amidotransferase C subunit; SPTR: Aspartyl-tRNA(Asn) amidotransferase subunit C / Glutamyl-tRNA(Gln) amidotransferase subunit C; TIGRFAM: glutamyl-tRNA(Gln) amidotransferase, C subunit; PFAM: Glu-tRNAGln amidotransferase C subunit; TIGRFAM: glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) amidotransferase, C subunit. (95 aa)    
Predicted Functional Partners:
gatB
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
 
 0.999
ADW19432.1
COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR004412: IPR000120: IPR020556; KEGG: dps:DP0643 glutamyl-tRNA(Gln) amidotransferase, subunit A; PFAM: Amidase; SPTR: Glutamyl-tRNA(Gln) amidotransferase subunit A; TIGRFAM: glutamyl-tRNA(Gln) amidotransferase, A subunit; PFAM: Amidase; TIGRFAM: glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) amidotransferase, A subunit.
 
 0.999
ADW17479.1
COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR004522: IPR006195: IPR004365: IPR004364: IPR 002312; KEGG: dps:DP1331 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase.
   
 0.977
glnS
COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR020060: IPR004514: IPR001412: IPR020058: IPR 020059; KEGG: dps:DP2738 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; SPTR: Probable glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; TIGRFAM: glutaminyl-tRNA synthetase.
  
 
 0.931
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
 
 0.890
ADW16702.1
COGs: COG0329 Dihydrodipicolinate synthase/N-acetylneuraminate lyase; InterPro IPR002220: IPR005263: IPR020624: IPR020625; KEGG: dps:DP0432 dihydrodipicolinate synthase; PFAM: dihydrodipicolinate synthetase; PRIAM: Dihydrodipicolinate synthase; SPTR: Dihydrodipicolinate synthase; TIGRFAM: dihydrodipicolinate synthase; PFAM: Dihydrodipicolinate synthetase family; TIGRFAM: dihydrodipicolinate synthase.
  
  
 0.819
atpH
ATP synthase F1 subcomplex delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
  
    0.799
ADW16956.1
COGs: COG0244 Ribosomal protein L10; InterPro IPR001790; KEGG: dps:DP1115 50S ribosomal protein L10; PFAM: ribosomal protein L10; SPTR: 50S ribosomal protein L10; PFAM: Ribosomal protein L10.
  
  
 0.782
ADW19434.1
COGs: COG0283 Cytidylate kinase; InterPro IPR003136: IPR011994; KEGG: dak:DaAHT2_2673 cytidylate kinase; PFAM: cytidylate kinase region; SPTR: Cytidylate kinase; TIGRFAM: cytidylate kinase; PFAM: Cytidylate kinase; TIGRFAM: cytidylate kinase.
  
    0.771
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
   
  
 0.755
Your Current Organism:
Desulfobulbus propionicus
NCBI taxonomy Id: 577650
Other names: D. propionicus DSM 2032, Desulfobulbus propionicus DSM 2032, Desulfobulbus propionicus str. DSM 2032, Desulfobulbus propionicus strain DSM 2032
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