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.
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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
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[Homology]
Score
pheTSimilar to Mycobacterium tuberculosis phenylalanyl-tRNA synthetase beta chain PheT or Rv1650 or MT1688 or MTCY06H11.15 SWALL:SYFB_MYCTU (SWALL:P94985) (831 aa) fasta scores: E(): 4.2e-156, 49.64% id in 844 aa, and to Bacillus subtilis phenylalanyl-tRNA synthetase beta chain PheT SWALL:SYFB_BACSU (SWALL:P17922) (804 aa) fasta scores: E(): 1.8e-53, 30.69% id in 847 aa. (836 aa)    
Predicted Functional Partners:
pheS
Similar to Mycobacterium tuberculosis phenylalanyl-tRNA synthetase alpha chain PheS or Rv1649 or MT1687 or MTCY06H11.14 SWALL:SYFA_MYCTU (SWALL:P94984) (341 aa) fasta scores: E(): 6.6e-87, 62.35% id in 340 aa, and to Bacillus subtilis phenylalanyl-tRNA synthetase alpha chain PheS SWALL:SYFA_BACSU (SWALL:P17921) (344 aa) fasta scores: E(): 2.6e-54, 44.02% id in 343 aa, and to Escherichia coli phenylalanyl-tRNA synthetase alpha chain PheS or B1714 SWALL:SYFA_ECOLI (SWALL:P08312) (327 aa) fasta scores: E(): 7.1e-52, 44.71% id in 331 aa; Belongs to the class-II aminoacyl-tRNA synthetase fa [...]
 
 0.999
DIP2130
Full length similarity to Streptococcus pneumoniae phosphoribosylformylglycinamidine synthase, putative SP0045 TR:AAK74234 (EMBL:AE007322) (1241 aa) fasta scores: E(): 7.8e-167, 47.73% id in 1259 aa. Second two thirds similar to many others e.g. Mycobacterium tuberculosis phosphoribosylformylglycinamidine synthase II PurL or Rv0803 or MT0823 or MTCY07H7A.06c SW:PURL_MYCTU (P54876) (754 aa) fasta scores: E(): 8.3e-22, 26.35% id in 740 aa.
  
  
 0.986
leuS
Similar to Escherichia coli leucyl-tRNA synthetase LeuS or B0642 SWALL:SYL_ECOLI (SWALL:P07813) (860 aa) fasta scores: E(): 1.9e-37, 37.53% id in 967 aa, and to Streptomyces coelicolor leucyl-tRNA synthetase LeuS SWALL:Q9RDL5 (EMBL:AL136518) (966 aa) fasta scores: E(): 1.6e-209, 59.93% id in 971 aa; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 0.977
ileS
isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
  
 
 0.964
guaA
GMP synthase [glutamine-hydrolysing]; Catalyzes the synthesis of GMP from XMP.
  
  
 0.950
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).
  
 
 0.946
argS
arginyl-tRNA synthetase; Similar to Mycobacterium tuberculosis arginyl-tRNA synthetase ArgS or Rv1292 or MT1331 or MTCY373.12 SW:SYR_MYCTU (Q10609) (550 aa) fasta scores: E(): 4.5e-144, 65.63% id in 550 aa, and to Bacillus subtilis arginyl-tRNA synthetase ArgS SW:SYR_BACSU (P46906) (556 aa) fasta scores: E(): 1.7e-82, 42.75% id in 545 aa.
  
  
 0.941
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.
 
 
 0.940
tyrS
tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.
  
  
 0.939
pyrD
Dihydroorotate dehydrogenase; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
  
  
 0.937
Your Current Organism:
Corynebacterium diphtheriae
NCBI taxonomy Id: 257309
Other names: C. diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC13129
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