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
alaSalanine--tRNA ligase; 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. (880 aa)    
Predicted Functional Partners:
pheT
KEGG: npu:Npun_F1087 0. phenylalanyl-tRNA synthetase, beta subunit K01890; Psort location: Cytoplasmic, score: 9.94.
 
 
 0.952
leuS
leucine--tRNA ligase; KEGG: npu:Npun_F4156 0. leucyl-tRNA synthetase K01869; Psort location: Cytoplasmic, score: 9.97; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.943
aspS
aspartate--tRNA ligase; 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.
  
 0.935
EKE96391.1
WD 40 repeat protein; KEGG: afm:AFUA_7G07100 8.4e-77 Pfs, NACHT and WD domain protein K00777.
   
 0.930
EKF02333.1
Tetratricopeptide repeat protein; KEGG: afm:AFUA_7G07100 1.1e-108 Pfs, NACHT and WD domain protein K00777; Psort location: OuterMembrane, score: 9.49.
   
 0.930
recA
Recombination protein A; 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.
 
 0.929
EKF00403.1
Putative heat shock protein DnaJ; KEGG: ava:Ava_4855 2.0e-57 WD-40 repeat-containing serine/threonin protein kinase K00908; Psort location: CytoplasmicMembrane, score: 9.50.
   
 0.905
EKF02051.1
Tetratricopeptide repeat protein; KEGG: cbb:CLD_1251 6.1e-14 pcrA; ATP-dependent DNA helicase PcrA K03657; Psort location: Cytoplasmic, score: 9.97.
   
  0.904
valS
valine--tRNA ligase; 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.
 
  
 0.887
EKF02266.1
Zinc finger found in FPG and IleRS; KEGG: npu:Npun_F1478 5.2e-09 isoleucyl-tRNA synthetase K01870.
  
 
 0.883
Your Current Organism:
Tolypothrix sp. PCC7601
NCBI taxonomy Id: 1188
Other names: Calothrix sp. PCC 7601, Fremyella diplosiphon ACMM 396, Fremyella diplosiphon IAM M-100, Fremyella diplosiphon UTEX B 481, Microchaete diplosiphon UTEX B 481, T. sp. PCC 7601, Tolypothrix (Calothrix) sp. PCC 7601, Tolypothrix sp. PCC 7601, Tolypothrix sp. PCC 7601 = UTEX B 481
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