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
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
metGmethionyl-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. (698 aa)    
Predicted Functional Partners:
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 2 subfamily.
 
 0.986
argS
arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 0.981
aspC
aspartyl-tRNA synthetase, archaeal type; 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).
 
 0.972
gltX
glutamyl-tRNA synthetase, archaeal and eukaryotic family; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
 
 0.963
proS
prolyl-tRNA synthetase, family I; 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).
 
 0.962
AGB31318.1
Cystathionine beta-lyase/cystathionine gamma-synthase; PFAM: Cys/Met metabolism PLP-dependent enzyme.
   
 
 0.928
AGB33106.1
PFAM: Pyruvate kinase, barrel domain; PEP-utilising enzyme, mobile domain; Pyruvate kinase, alpha/beta domain; TIGRFAM: pyruvate kinase; Belongs to the pyruvate kinase family.
     
 0.926
AGB31326.1
Methionine synthase II (cobalamin-independent); PFAM: Cobalamin-independent synthase, N-terminal domain.
    
 0.913
AGB31327.1
Methionine synthase II (cobalamin-independent); PFAM: Cobalamin-independent synthase, Catalytic domain.
    
 0.913
tyrS
tyrosyl-tRNA synthetase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily.
 
 
 0.872
Your Current Organism:
Natrinema pellirubrum
NCBI taxonomy Id: 797303
Other names: N. pellirubrum DSM 15624, Natrinema pellirubrum DSM 15624, Natrinema pellirubrum JCM 10476, Natrinema pellirubrum NCIMB 786, Natrinema pellirubrum str. DSM 15624, Natrinema pellirubrum strain DSM 15624
Server load: low (34%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.