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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
hisSCOGs: 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. (417 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.
 
  
 0.967
hisG
ATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
  
 
 0.884
Deba_0397
Tetratricopeptide TPR_2 repeat protein; InterProIPR011717:IPR013105:IPR019734:IPR011990:IPR 013026; KEGG: dal:Dalk_1963 TPR repeat-containing protein; PFAM: Tetratricopeptide TPR_2 repeat protein; Tetratricopeptide TPR_4; SMART: Tetratricopeptide repeat; SPTR: B8FEY2 TPR repeat-containing protein; PFAM: Tetratricopeptide repeat.
  
    0.823
glyQ
COGs: COG0752 Glycyl-tRNA synthetase alpha subunit; InterPro IPR002310:IPR006194; KEGG: sat:SYN_01536 glycyl-tRNA synthetase subunit alpha; PFAM: glycyl-tRNA synthetase alpha subunit; PRIAM: Glycine--tRNA ligase; SPTR: Q2LVI0 Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; PFAM: Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, alpha subunit.
  
  
 0.816
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 [...]
  
 
 0.813
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.
 
 
 0.811
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.
 
 
 0.809
Deba_2879
COGs: COG3276 Selenocysteine-specific translation elongation factor; InterProIPR000795:IPR004161:IPR015190:IPR015191:IPR 011991:IPR009000:IPR009001:IPR005225:IPR004535; KEGG: dal:Dalk_1105 selenocysteine-specific translation elongation factor; PFAM: protein synthesis factor GTP-binding; elongation factor Tu domain 2 protein; Elongation factor SelB winged helix 2; Elongation factor SelB winged helix 3; SPTR: B8F962 Selenocysteine-specific translation elongation factor; TIGRFAM: selenocysteine-specific translation elongation factor; small GTP-binding protein; PFAM: Elongation factor Tu C [...]
   
 0.809
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.
 
 
 0.801
lysS
COGs: COG1190 Lysyl-tRNA synthetase (class II); InterProIPR018149:IPR004365:IPR004364:IPR016027:IPR 006195:IPR012340:IPR002313; KEGG: drt:Dret_2234 lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: C8X521 Lysyl-tRNA synthetase; TIGRFAM: lysyl-tRNA synthetase; 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 synthetase family.
 
 
 0.774
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
Server load: low (14%) [HD]