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.
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
hisSTIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; KEGG: pis:Pisl_1621 histidyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (427 aa)    
Predicted Functional Partners:
Cmaq_1359
PFAM: RNA binding S1 domain protein; Eukaryotic translation initiation factor 2, alpha subunit; KEGG: pis:Pisl_0433 translation initiation factor 2, alpha subunit.
   
 0.960
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). Also edits incorrectly charged L-seryl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.927
rpl2
Ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
 
 
 0.912
Cmaq_1531
PFAM: protein synthesis factor GTP-binding; elongation factor Tu domain 2 protein; Initiation factor eIF2 gamma, C terminal; KEGG: pis:Pisl_0078 protein synthesis factor, GTP-binding.
  
 0.905
Cmaq_0166
aminoacyl-tRNA synthetase class Ia; KEGG: pai:PAE2297 valyl-tRNA synthetase.
 
 
 0.894
cysS
TIGRFAM: cysteinyl-tRNA synthetase; PFAM: Cysteinyl-tRNA synthetase class Ia DALR; tRNA synthetase class I (M); Cysteinyl-tRNA synthetase class Ia; KEGG: pis:Pisl_1108 cysteinyl-tRNA synthetase.
 
 
 0.887
leuS
leucyl-tRNA synthetase; Good alignment up to ATA codon, potential RBS upstream; TIGRFAM: leucyl-tRNA synthetase; KEGG: pab:PAB1782 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.882
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.
  
 
 0.880
Cmaq_0608
TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase class IIc; KEGG: tpe:Tpen_0950 phenylalanyl-tRNA synthetase, alpha subunit.
 
  
 0.875
Cmaq_1197
TIGRFAM: isoleucyl-tRNA synthetase; KEGG: pis:Pisl_1650 isoleucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
  
 0.873
Your Current Organism:
Caldivirga maquilingensis
NCBI taxonomy Id: 397948
Other names: C. maquilingensis IC-167, Caldivirga maquilingensis DSM 13496, Caldivirga maquilingensis IC-167, Caldivirga maquilingensis JCM 10307, Caldivirga maquilingensis str. IC-167, Caldivirga maquilingensis strain IC-167
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.