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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
tilStRNA(Ile)-lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family. (324 aa)    
Predicted Functional Partners:
hprT
Hypoxanthine phosphoribosyltransferase; Acts preferentially on hypoxanthin; has very low activity towards guanine. Inactive towards xanthine (By similarity); Belongs to the purine/pyrimidine phosphoribosyltransferase family; KEGG: nfa:nfa3890 hypoxanthine phosphoribosyltransferase.
 
  
 0.982
APA94431.1
Hypothetical protein.
     
 0.904
dacB
Hypothetical protein.
 
   
 0.904
thiS
Hypothetical protein.
  
 
 0.814
iarS
Isoleucine--tRNA ligase; 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.
  
  
 0.791
mfd
Transcription-repair-coupling factor; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site; In the C-terminal section; belongs to the helicase family. RecG subfamily.
 
  
 0.706
pheT
Phenylalanine--tRNA ligase; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily; Contains 1 B5 domain; Contains 1 FDX-ACB domain; Contains 1 tRNA-binding domain; KEGG: asd:AS9A_1504 phenylalanyl-tRNA synthetase beta chain.
 
   
 0.695
ppa
Inorganic diphosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
     
 0.686
lysS
Lysine--tRNA ligase; Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M. tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine resu [...]
   
 
 0.681
pth1
Aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family.
  
  
 0.671
Your Current Organism:
Nocardia seriolae
NCBI taxonomy Id: 37332
Other names: ATCC 43993, CCUG 46828, CIP 104778, DSM 44129, IFO 15557, JCM 3360, N. seriolae, NBRC 15557
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