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
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. (882 aa)    
Predicted Functional Partners:
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.
  
 0.927
Chro_4160
Tetratricopeptide TPR_1 repeat-containing protein; PFAM: Tetratricopeptide repeat; COGs: COG0457 FOG: TPR repeat; InterPro IPR019734:IPR013026:IPR001440; KEGG: amr:AM1_G0032 TPR repeat-containing protein; PFAM: Tetratricopeptide TPR_1 repeat-containing protein; SMART: Tetratricopeptide repeat; SPTR: TPR repeat protein.
  
 0.916
pheT
phenylalanyl-tRNA synthetase beta subunit; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR002547:IPR005121:IPR004532:IPR005146:IPR 005147; KEGG: npu:Npun_F1087 phenylalanyl-tRNA synthetase subunit beta; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; PRIAM: Phenylalanine--tRNA ligase; SPTR: Phenyla [...]
 
 
 0.886
leuS
PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302:IPR015413:IPR013155:IPR001412; KEGG: ana:alr3283 leucyl-tRNA synthetase; PFAM: tRNA synthetase valyl/leucyl anticodon-binding; tRNA synthetase class I (M); SPTR: Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.873
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; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
 
  
 0.860
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 1 subfamily.
 
 
 0.816
glyQ
PFAM: Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, alpha subunit; COGs: COG0752 Glycyl-tRNA synthetase alpha subunit; InterPro IPR006194:IPR002310; KEGG: naz:Aazo_0922 glycyl-tRNA synthetase subunit alpha; PFAM: glycyl-tRNA synthetase alpha subunit; PRIAM: Glycine--tRNA ligase; SPTR: Glycyl-tRNA synthetase, alpha subunit; TIGRFAM: glycyl-tRNA synthetase, alpha subunit.
  
  
 0.789
glyS
PFAM: Glycyl-tRNA synthetase beta subunit; DALR anticodon binding domain; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, beta subunit; COGs: COG0751 Glycyl-tRNA synthetase beta subunit; InterPro IPR002311:IPR008909:IPR015944:IPR006194; KEGG: ava:Ava_0794 glycyl-tRNA synthetase subunit beta; PFAM: glycyl-tRNA synthetase beta subunit; DALR anticodon binding domain protein; PRIAM: Glycine--tRNA ligase; SPTR: Glycyl and Arginyl tRNA synthetase; TIGRFAM: glycyl-tRNA synthetase, beta subunit.
 
  
 0.777
ftsY
Signal recognition particle-docking protein FtsY; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
 
  
 0.740
prfA
Bacterial peptide chain release factor 1 (bRF-1); Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
 
 
 0.739
Your Current Organism:
Chroococcidiopsis thermalis
NCBI taxonomy Id: 251229
Other names: C. thermalis PCC 7203, Chroococcidiopsis sp. ATCC 27900, Chroococcidiopsis sp. PCC 7203, Chroococcidiopsis thermalis PCC 7203, Chroococcidiopsis thermalis str. PCC 7203
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