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.
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colored nodes:
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
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
gatCaspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; 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 GatC family. (97 aa)    
Predicted Functional Partners:
gatA
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln).
 
 0.999
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
asnS
COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR002312: IPR004522: IPR006195: IPR004365: IPR 004364; KEGG: xal:XALc_1738 probable asparaginyl-tRNA synthetase (AsnRS) protein; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Probable asparaginyl-trna synthetase (Asnrs) protein; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase.
   
 0.964
Isop_0766
Gas vesicle synthesis GvpLGvpF; InterPro IPR009430; KEGG: mxa:MXAN_2769 GvpL/GvpF family gas vesicle protein; PFAM: Gas vesicle synthesis GvpLGvpF; SPTR: Putative gas vesicle synthesis GvpLGvpF; PFAM: Gas vesicle synthesis protein GvpL/GvpF.
  
 
 0.900
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.
  
 
 0.825
atpH
ATP synthase F1, 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; Belongs to the ATPase delta chain family.
 
    0.711
Isop_2214
Glutamate synthase (NADH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR000583: IPR006982: IPR002932: IPR002489: IPR 017932; KEGG: ttr:Tter_0474 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Glutamate synthase (Ferredoxin); PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II.
   
 
 0.665
rpsZ
SSU ribosomal protein S14P; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
   
    0.659
dapA
Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
  
  
 0.640
Isop_1578
COGs: COG0329 Dihydrodipicolinate synthase/N-acetylneuraminate lyase; InterPro IPR002220: IPR005829; KEGG: psl:Psta_3336 dihydrodipicolinate synthetase; PFAM: dihydrodipicolinate synthetase; SPTR: Dihydrodipicolinate synthetase; PFAM: Dihydrodipicolinate synthetase family; Belongs to the DapA family.
  
  
 0.640
Your Current Organism:
Isosphaera pallida
NCBI taxonomy Id: 575540
Other names: I. pallida ATCC 43644, Isosphaera pallida ATCC 43644, Isosphaera pallida DSM 9630, Isosphaera pallida IS1B, Isosphaera pallida str. ATCC 43644, Isosphaera pallida strain ATCC 43644
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