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
gatCglutamyl-tRNA (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. (91 aa)    
Predicted Functional Partners:
gatB
glutamyl-tRNA(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
gatA
Glutamyl-tRNA(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
asnS
asparaginyl-tRNA synthetase; PMID: 2693216 PMID: 1425658 PMID: 2009959 PMID: 1544480 best DB hits: BLAST: swissprot:P52276; SYN_SYNY3 PROBABLE ASPARAGINYL-TRNA SYNTHETASE; E=1e-151 gb:AAK02727.1; (AE006100) AsnS [Pasteurella multocida]; E=1e-150 pir:E82217; asparaginyl-tRNA synthetase VC1297 [imported] - Vibrio; E=1e-148 COG: sll0495; COG0017 Aspartyl/asparaginyl-tRNA synthetases; E=1e-152 PFAM: PF01336; OB-fold nucleic acid binding dom; E=6.8e-15 PF01409; tRNA synthetases class II (F); E=0.025 PF00152; tRNA synthetases class II (D, K; E=1.3e-132.
   
 0.955
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.
  
 
 0.927
glnS
glutaminyl-tRNA synthetase; PMID: 10984043 best DB hits: BLAST: pir:F83421; glutaminyl-tRNA synthetase PA1794 [imported] -; E=0.0 pdb:1QRU; A Chain A, Glutaminyl-Trna Synthetase Mutant I129t; E=1e-179 pdb:1QRS; A Chain A, Glutaminyl-Trna Synthetase Mutant D235n; E=1e-178 COG: PA1794; COG0008 Glutamyl- and glutaminyl-tRNA synthetases; E=0.0 PFAM: PF00749; tRNA synthetases class I (E and; E=1.2e-179.
  
 
 0.918
rpsN
30 S ribosomal protein S14; 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.
   
    0.804
atpD
Probable ATP synthase delta chain; 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.
  
    0.754
rplJ
PMID: 8969501 best DB hits: BLAST: pir:T01743; ribosomal protein L10, chloroplast - common tobacco; E=3e-08 swissprot:P42923; RL10_BACSU 50S RIBOSOMAL PROTEIN L10 (BL5) (COLD; E=3e-08 gb:AAK05367.1; AE006359_5 (AE006359) 50S ribosomal protein L10; E=8e-08 COG: BS_rplJ; COG0244 Ribosomal protein L10; E=3e-09.
   
    0.734
rplA
50S ribosomal protein L1; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
   
    0.709
gltB
Glutamate synthase [NADPH] large chain; PMID: 2643092 PMID: 3326786 best DB hits: BLAST: swissprot:Q06434; GLSF_ANTSP FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE; E=0.0 swissprot:P23225; GLSF_MAIZE FERREDOXIN-DEPENDENT GLUTAMATE; E=0.0 swissprot:Q03460; GLSN_MEDSA GLUTAMATE SYNTHASE [NADH], CHLOROPLAST; E=0.0 COG: sll1502_2; COG0069 Glutamate synthetase domain 2; E=0.0 sll1502_1; COG0067 Glutamate synthetase domain 1; E=1e-118 PFAM: PF01645; Conserved region in glutamate; E=5.5e-235 PF01493; Domain of unknown function DU; E=4.2e-95.
   
 
 0.684
Your Current Organism:
Rhodopirellula baltica
NCBI taxonomy Id: 243090
Other names: Pirellula sp. 1, R. baltica SH 1, Rhodopirellula baltica SH 1, Rhodopirellula baltica str. SH 1, Rhodopirellula baltica strain SH 1
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