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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
serSseryl-tRNA synthetase (serS); Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). (521 aa)    
Predicted Functional Partners:
sepS
phenylalanyl-tRNA synthase alpha subunit; Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).
 
 
 0.986
argS
arginyl-tRNA synthetase (argS); Identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.966
MJ_0158
Selenocystein synthase (selA); Similar to SP:P23328 GB:M64177 PID:147804 PID:466729 GB:U00096 percent identity: 34.65; identified by sequence similarity; putative; Belongs to the UPF0425 family.
    
 0.941
pstK
Yeast KTI12 Protein; Specifically phosphorylates seryl-tRNA(Sec) to O- phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine biosynthesis.
  
 
 0.939
valS
valyl-tRNA synthetase (valS); 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 2 subfamily.
  
  
 0.890
trpS
tryptophanyl-tRNA synthetase (trpS); Similar to GB:X59892 GB:X67918 GB:X67919 GB:X67920 GB:X67921 percent identity: 31.02; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.888
MJ_1130
O-sialoglycoprotein endopeptidase (gcp); Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction (By similarity). The Bud32 domain probably displays kinase activity that regulates Kae1 function. In vitro, exhibits low ATPase activity, but does not bind DNA and does [...]
  
  
 0.851
tyrS
tyrosyl-tRNA synthetase (trS); Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
  
  
 0.845
pheS
phenylalanyl-tRNA synthetase, subunit alpha (pheS); Similar to SP:P15625 PID:172947 PID:836732 percent identity: 40.91; identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
 
  
 0.810
leuS
leucyl-tRNA synthetase (leuS); Similar to SP:P26637 PID:1370340 PID:1403549 PID:3508 percent identity: 35.17; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
  
 0.809
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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