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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[Homology]
Score
alaSAlanyl-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. (893 aa)    
Predicted Functional Partners:
CCH88751.1
Putative Holliday junction resolvase; Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA; Belongs to the YqgF HJR family.
 
  
 0.970
pheT
Phenylalanyl-tRNA synthetase beta chain; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
 
 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.
  
 0.933
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.
 
  
 0.900
CCH90165.1
Putative Transcriptional regulator; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator.
  
 0.893
mltG
Protein of unknown function; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. Belongs to the transglycosylase MltG family.
  
    0.879
leuS
Leucyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.837
aroE-2
Shikimate dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the shikimate dehydrogenase family.
  
    0.836
thrS
Threonyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.828
efp
Elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
 
  
 0.816
Your Current Organism:
Modestobacter marinus
NCBI taxonomy Id: 477641
Other names: CGMCC 4.5581, DSM 45201, M. marinus, Modestobacter marinus Xiao et al. 2011, Modestobacter sp. 42H12-1, strain 42H12-1
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