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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
SCO1501Alanine 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. (890 aa)    
Predicted Functional Partners:
SCO1500
Conserved hypothetical protein; Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA; Belongs to the YqgF nuclease family.
 
  
 0.973
SCO1594
SCI35.16c, pheT, proabable phenylalanyl-tRNA synthetase beta chain, len: 840 aa; similar to many e.g. SYFB_ECOLI phenylalanyl-tRNA synthetase beta chain (EC 6.1.1.20) (795 aa), fasta scores; opt: 988 z-score: 1290.9 E(): 0, 36.0% identity in 849 aa overlap. Contains PS00017 ATP/GTP-binding.
 
 
 0.941
SCO1502
SC9C5.26c, possible secreted protein, len: 118 aa. Contains possible N-terminal signal peptide sequence.
       0.875
SCO1503
SC9C5.27c, possible secreted protein, len: 149 aa. Contains possible N-terminal region signal peptide sequence.
       0.875
SCO2615
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.
 
  
 0.838
SCO1531
threonine-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).
  
 
 0.815
SCO3795
aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
  
 0.812
SCO2571
SCC123.09c, leuS, leucyl-tRNA synthetase (EC 6.1.1.4) len: 966 aa. Highly similar to many leucyl-tRNA synthetases including: Bacillus subtilis SW:SYL_BACSU(EMBL:M88581) (804 aa), fasta scores opt: 508 z-score: 575.2 E(): 1.2e-24 48.1% identity in 941 aa overlap and Mycobacterium leprae SW:SYL_MYCLE(EMBL:Y14967) (972 aa), fasta scores opt: 3887 z-score: 4430.5 E():0 60.1% identity in 977 aa overlap. Contains a Prosite hit to PS00178 Amino-acyl-transfer RNA synthetases class-I signature and a Pfam match to entry PF00133 tRNA-synt_1, tRNA synthetases class I (I, L, M and V).
  
 
 0.802
SCO1504
SC9C5.28, putative regulator, len: 750 aa; similar to TR:O53720 (EMBL:AL021931) Mycobacterium tuberculosis transcriptional regulatory protein MTV036.21, 1085 aa; fasta scores: opt: 975 z-score: 1090.3 E(): 0; 34.3% identity in 724 aa overlap. Contains match to Prosite entry PS00017 ATP/GTP-binding site motif A (P-loop).
       0.787
SCO6160
Putative SecDF protein-export membrane protein; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily.
  
    0.786
Your Current Organism:
Streptomyces coelicolor
NCBI taxonomy Id: 100226
Other names: S. coelicolor A3(2), Streptomyces coelicolor A3(2)
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.