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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
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. (876 aa)    
Predicted Functional Partners:
pheT
COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; InterProIPR004532:IPR002547:IPR005146:IPR005147:IPR 005121; KEGG: phe:Phep_0825 phenylalanyl-tRNA synthetase subunit beta; PFAM: B3/B4 tRNA-binding domain; tRNA-binding region; tRNA synthetase, B5; Phenylalanyl-tRNA synthetase, beta subunit, ferrodoxin-fold anticodon-binding; SPTR: Phenylalanine--tRNA ligase; TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; IMG reference gene:2504772211; PFAM: tRNA synthetase B5 domain; B3/4 domain; [...]
 
 
 0.871
metG
Methionyl-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.
 
  
 0.857
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.
 
  
 0.856
thrS
threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr).
  
 
 0.830
leuS
COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR015413:IPR013155:IPR002302; KEGG: sli:Slin_1712 leucyl-tRNA synthetase; PFAM: Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding; Aminoacyl-tRNA synthetase, class I (M); PRIAM: Leucine--tRNA ligase; SPTR: Leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; IMG reference gene:2504770101; PFAM: tRNA synthetases class I (I, L, M and V); tRNA synthetases class I (M); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family.
 
 
 0.817
secF
Protein-export membrane protein SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily.
  
    0.808
aspS
aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
  
 0.803
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.
 
 
 0.784
AEE51863.1
COGs: COG0172 Seryl-tRNA synthetase; InterPro IPR015866:IPR002314:IPR002317; KEGG: coc:Coch_0734 seryl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Seryl-tRNA synthetase, class IIa, N-terminal; PRIAM: Serine--tRNA ligase; SPTR: Serine--tRNA ligase; TIGRFAM: Seryl-tRNA synthetase, class IIa; IMG reference gene:2504773400; PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase.
  
 
 0.778
lysS
COGs: COG1190 Lysyl-tRNA synthetase (class II); HAMAP: Lysyl-tRNA synthetase; InterPro IPR004365:IPR004364:IPR002313; KEGG: phe:Phep_1559 lysyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Lysine--tRNA ligase; SPTR: Lysyl-tRNA synthetase; TIGRFAM: Lysyl-tRNA synthetase, class II; IMG reference gene:2504770647; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; Belongs to the class-II aminoacyl-tRNA synt [...]
 
 
 0.736
Your Current Organism:
Haliscomenobacter hydrossis
NCBI taxonomy Id: 760192
Other names: H. hydrossis DSM 1100, Haliscomenobacter hydrossis DSM 1100
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