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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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. (894 aa)    
Predicted Functional Partners:
ADV68245.1
Alanyl-tRNA synthetase, class IIc; COGs: COG2872 metal-dependent hydrolase related to alanyl-tRNA synthetase HxxxH domain; InterPro IPR018164: IPR012947: IPR003156; KEGG: dge:Dgeo_1201 threonyl/alanyl tRNA synthetase, SAD; PFAM: Alanyl-tRNA synthetase, class IIc, N-terminal; Threonyl/alanyl tRNA synthetase, SAD; Phosphoesterase, DHHA1; SMART: Threonyl/alanyl tRNA synthetase, SAD; SPTR: Threonyl/alanyl tRNA synthetase, SAD; PFAM: DHHA1 domain; Threonyl and Alanyl tRNA synthetase second additional domain; tRNA synthetases class II (A).
  
 
0.923
pheT
COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; InterProIPR005146: IPR005147: IPR005121: IPR004532: IPR 002547; KEGG: dge:Dgeo_0224 phenylalanyl-tRNA synthetase subunit beta; PFAM: B3/B4 tRNA-binding domain; tRNA-binding domain; tRNA synthetase, B5; Phenylalanyl-tRNA synthetase, beta subunit, ferrodoxin-fold anticodon-binding; SMART: B3/B4 tRNA-binding domain; tRNA synthetase, B5; Phenylalanyl-tRNA synthetase, beta subunit, ferrodoxin-fold anticodon-binding; SPTR: Phenylalanyl-tRNA synthetase, beta subuni [...]
 
 
 0.849
ADV68057.1
Hypothetical protein; KEGG: scl:sce2686 WD repeat-containing protein; SPTR: Putative WD-40 repeat protein.
  
 0.829
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.
 
  
 0.811
leuS
COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302: IPR015413: IPR013155; KEGG: dge:Dgeo_0567 leucyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class I (M); Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding; SPTR: Leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family.
 
 
 0.809
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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily.
  
  
 0.809
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.
  
  
 0.788
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.
  
 
 0.770
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).
  
 
 0.714
glyQS
glycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.689
Your Current Organism:
Deinococcus maricopensis
NCBI taxonomy Id: 709986
Other names: D. maricopensis DSM 21211, Deinococcus maricopensis DSM 21211, Deinococcus maricopensis LB-34, Deinococcus maricopensis str. DSM 21211, Deinococcus maricopensis strain DSM 21211
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