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:
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Cooccurrence
Coexpression
Experiments
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[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. (884 aa)    
Predicted Functional Partners:
pheT
COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR004532:IPR002547:IPR005121:IPR012340:IPR 020825:IPR005147:IPR016027:IPR009061:IPR005146; KEGG: sfu:Sfum_0429 phenylalanyl-tRNA synthetase, beta subunit; PFAM: B3/4 domain protein; t-RNA-binding domain protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: A0LFC7 Phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: 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 synth [...]
 
 
 0.917
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.
  
  
 0.908
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.
 
  
 0.875
Deba_1143
Competence/damage-inducible protein CinA; COGs: COG1546 Uncharacterized protein (competence- and mitomycin-induced); InterPro IPR001453:IPR008136:IPR008135; KEGG: gme:Gmet_0196 competence/damage-inducible protein CinA; PFAM: CinA domain protein; molybdopterin binding domain; SPTR: C8QYB6 Competence/damage-inducible protein CinA; TIGRFAM: competence/damage-inducible protein CinA; PFAM: Probable molybdopterin binding domain; Competence-damaged protein; TIGRFAM: competence/damage-inducible protein CinA N-terminal domain; competence/damage-inducible protein CinA C-terminal domain; molybden [...]
  
    0.858
recA
recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
  
  
 0.849
leuS
COGs: COG0495 Leucyl-tRNA synthetase; InterProIPR015945:IPR013155:IPR001412:IPR014729:IPR 002302:IPR009008:IPR009080; KEGG: glo:Glov_2116 leucyl-tRNA synthetase; PFAM: tRNA synthetase valyl/leucyl anticodon-binding; Arginyl-tRNA synthetase, class Ic, core; SPTR: B3E3L3 Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.839
Deba_3097
Tetratricopeptide TPR_2 repeat protein; InterProIPR001440:IPR013105:IPR019734:IPR013026:IPR 011990; KEGG: dat:HRM2_20780 tetratricopeptide (TPR) domain protein; PFAM: Tetratricopeptide TPR_2 repeat protein; TPR repeat-containing protein; SPTR: C0QDB3 Tetratricopeptide (TPR) domain protein; PFAM: ChAPs (Chs5p-Arf1p-binding proteins); TIGRFAM: putative PEP-CTERM system TPR-repeat lipoprotein.
  
 0.830
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.
  
  
 0.820
thrS
COGs: COG0441 Threonyl-tRNA synthetase; InterProIPR002320:IPR006195:IPR004154:IPR018163:IPR 018158:IPR012947:IPR002314; KEGG: dde:Dde_2639 threonyl-tRNA synthetase / Ser-tRNA(Thr) hydrolase; PFAM: tRNA synthetase class II (G H P and S); Threonyl/alanyl tRNA synthetase SAD; Anticodon-binding domain protein; SPTR: Q30Y11 Threonyl-tRNA synthetase; TIGRFAM: threonyl-tRNA synthetase; PFAM: Anticodon binding domain; Threonyl and Alanyl tRNA synthetase second additional domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: threonyl-tRNA synthetase; Belongs to the class-II [...]
  
 
 0.801
hisS
COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR015807:IPR006195:IPR004154:IPR002314:IPR 004516; KEGG: ppd:Ppro_1381 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: A1ANS7 Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; manually curated; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase.
 
 
 0.786
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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