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
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
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Neighborhood
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Co-expression
Experiments
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[Homology]
Score
asnSasparaginyl-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. (490 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.
 
 0.997
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).
   
 0.985
metG
methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
 0.976
gatC
glutamyl-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.
   
 0.968
proS
Prolyl tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
  
 0.967
lueS
Putative leucyl-tRNA synthetase; PMID: 1317842 best DB hits: BLAST: ddbj:BAB17162.1; (AP002868) putative leucyl-tRNA synthetase; E=0.0 embl:CAB77903.1; (AL161500) putative leucyl tRNA synthetase; E=0.0 gb:AAK04914.1; AE006315_3 (AE006315) leucyl-tRNA synthetase (EC; E=0.0 COG: TP0586; COG0495 Leucyl-tRNA synthetase; E=0.0 PFAM: PF00133; tRNA synthetases class I (I, L; E=1.4e-39; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.957
argS
arginyl-tRNA synthetase; PMID: 2668891 best DB hits: BLAST: pir:G82121; arginyl-tRNA synthetase VC2074 [imported] - Vibrio; E=1e-69 swissprot:Q55486; SYR_SYNY3 ARGINYL-TRNA SYNTHETASE; E=5e-68 embl:CAC01600.1; (AJ269505) putative arginyl-tRNA synthetase; E=4e-66 COG: VC2074; COG0018 Arginyl-tRNA synthetase; E=1e-70 PFAM: PF00750; tRNA synthetases class I (R); E=5.7e-55.
   
 0.942
gluQ
glutamyl-tRNA synthetase-related protein; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.
  
 0.941
ileS
Probable isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
   
 0.937
lysS
lysyl-tRNA synthetase; Best DB hits: BLAST: swissprot:Q53638; SYK_STAAU LYSYL-TRNA SYNTHETASE (LYSINE--TRNA; E=1e-116 swissprot:P37477; SYK_BACSU LYSYL-TRNA SYNTHETASE (LYSINE--TRNA; E=1e-114 swissprot:Q9KGG4; SYK_BACHD LYSYL-TRNA SYNTHETASE (LYSINE--TRNA; E=1e-111 COG: BS_lysS; COG1190 Lysyl-tRNA synthetase class II; E=1e-115 PFAM: PF01336; OB-fold nucleic acid binding dom; E=5.9e-12 PF01409; tRNA synthetases class II (F); E=0.46 PF00152; tRNA synthetases class II (D, K; E=7e-136; Belongs to the class-II aminoacyl-tRNA synthetase family.
   
 0.911
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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