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
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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
glySglycyl-tRNA synthetase, beta subunit; Identified by similarity to SP:P00961; match to protein family HMM PF02092; match to protein family HMM PF05746; match to protein family HMM TIGR00211. (693 aa)    
Predicted Functional Partners:
glyQ
glycyl-tRNA synthetase, alpha subunit; Identified by similarity to SP:P00960; match to protein family HMM PF02091; match to protein family HMM TIGR00388.
 0.999
MCA2051
Hydrolase, HAD-superfamily, subfamily IIIA; Identified by match to protein family HMM TIGR01656; match to protein family HMM TIGR01662.
       0.817
MCA2052
Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase; Identified by similarity to OMNI:NTL03PA00006; match to protein family HMM PF01553.
       0.817
ileS
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 1 subfamily.
 
  
 0.806
leuS
leucyl-tRNA synthetase; Identified by match to protein family HMM PF00133; match to protein family HMM TIGR00396; Belongs to the class-I aminoacyl-tRNA synthetase family.
   
  
 0.783
alaS
alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
 
  
 0.777
valS
valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
  
  
 0.777
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.
  
  
 0.650
pheT
phenylalanyl-tRNA synthetase, beta subunit; Identified by similarity to SP:P07395; match to protein family HMM PF01588; match to protein family HMM PF03147; match to protein family HMM PF03483; match to protein family HMM PF03484; match to protein family HMM TIGR00472; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.612
speA
Arginine decarboxylase; Catalyzes the biosynthesis of agmatine from arginine.
       0.605
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
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