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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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
hisSPFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase; COGs: COG0124 Histidyl-tRNA synthetase; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; InterPro IPR015807:IPR002314:IPR004154; KEGG: sta:STHERM_c15800 histidyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Anticodon-binding; SPTR: Histidyl-tRNA synthetase; TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup. (437 aa)    
Predicted Functional Partners:
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. Short subfamily.
 
 
 0.894
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.
  
  
 0.885
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.
 
 
 0.753
alaS
alanyl-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.
 
 
 0.748
AEJ61894.1
Helicase-associated domain protein; PFAM: Helicase conserved C-terminal domain; Helicase associated domain (HA2); Domain of unknown function (DUF1605); DEAD/DEAH box helicase; TIGRFAM: ATP-dependent helicase HrpA; COGs: COG1643 HrpA-like helicase; InterPro IPR014001:IPR001650:IPR007502:IPR011709; KEGG: sta:STHERM_c15810 hypothetical protein; PFAM: Helicase-associated region; DNA/RNA helicase, C-terminal; Domain of unknown function DUF1605; SMART: DEAD-like helicase, N-terminal; DNA/RNA helicase, C-terminal; SPTR: Helicase-associated domain protein.
   
 0.732
argS
Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR005148:IPR015945:IPR008909:IPR001278; KEGG: sta:STHERM_c10230 hypothetical protein; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic.
 
  
 0.710
ispG
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family.
  
  
 0.678
AEJ61892.1
PFAM: Poly A polymerase head domain; TIGRFAM: poly(A) polymerase; COGs: COG0617 tRNA nucleotidyltransferase/poly(A) polymerase; InterPro IPR010206:IPR002646; KEGG: sta:STHERM_c15790 polyA polymerase family protein; PFAM: Polynucleotide adenylyltransferase region; SPTR: Poly(A) polymerase; TIGRFAM: Poly(A) polymerase, PcnB.
  
  
 0.637
pheS
PFAM: tRNA synthetases class II core domain (F); TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; COGs: COG0016 Phenylalanyl-tRNA synthetase alpha subunit; HAMAP: Phenylalanyl-tRNA synthetase alpha chain; InterPro IPR004529:IPR002319; KEGG: sta:STHERM_c21750 phenylalanyl-tRNA synthetase, alpha subunit; PFAM: Phenylalanyl-tRNA synthetase alpha chain; SPTR: Phenylalanyl-tRNA synthetase alpha chain; TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
 
  
 0.633
thrS
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; COGs: COG0441 Threonyl-tRNA synthetase; InterPro IPR002320:IPR012947:IPR002314:IPR004154; KEGG: sta:STHERM_c16030 threonyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Threonyl/alanyl tRNA synthetase, SAD; Anticodon-binding; SPTR: Ser-tRNA(Thr) hydrolase; threonyl-tRNA synthetase; TIGRFAM: Threonyl-tRNA synthetase, class IIa; Belong [...]
 
 
 0.622
Your Current Organism:
Spirochaeta thermophila
NCBI taxonomy Id: 869211
Other names: S. thermophila DSM 6578, Spirochaeta thermophila DSM 6578, Spirochaeta thermophila str. DSM 6578, Spirochaeta thermophila strain DSM 6578
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