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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ORA83048.1aminoacyl-tRNA deacylase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. (169 aa)    
Predicted Functional Partners:
ORA83049.1
RNA polymerase subunit sigma; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the sigma-70 factor family. ECF subfamily.
       0.650
ORA83050.1
Mycothiol system anti-sigma-R factor; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.650
aspS
aspartate--tRNA ligase; 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.
    
 0.551
proS
proline--tRNA ligase; 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...]
     
 0.447
Your Current Organism:
Mycolicibacter kumamotonensis
NCBI taxonomy Id: 354243
Other names: CCUG 51961, DSM 45093, GTC 2729, JCM 13453, M. kumamotonensis, Mycobacterium kumamotoense, Mycobacterium kumamotonense, Mycobacterium kumamotonense Masaki et al. 2007, Mycolicibacter kumamotonensis (Masaki et al. 2007) Gupta et al. 2018, strain CST 7247
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