STRINGSTRING
leuS leuS pheT pheT metG metG AII45950.1 AII45950.1 tyrS tyrS argS argS lysS lysS ileS ileS gltX gltX proS proS pheS pheS
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:
leuSleucyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: GeneMarkS+; Belongs to the class-I aminoacyl-tRNA synthetase family. (858 aa)
pheTphenylalanyl-tRNA synthetase subunit beta; Derived by automated computational analysis using gene prediction method: GeneMarkS+; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (813 aa)
metGmethionyl-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. (514 aa)
AII45950.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+; Belongs to the class-I aminoacyl-tRNA synthetase family. (291 aa)
tyrStyrosyl-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 2 subfamily. (415 aa)
argSarginyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (590 aa)
lysSlysyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: GeneMarkS+; Belongs to the class-II aminoacyl-tRNA synthetase family. (503 aa)
ileSisoleucyl-tRNA synthase; 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 1 subfamily. (973 aa)
gltXglutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (477 aa)
proSprolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] (593 aa)
pheSphenylalanyl-tRNA synthetase subunit alpha; Derived by automated computational analysis using gene prediction method: GeneMarkS+; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (335 aa)
Your Current Organism:
Synechococcus sp. KORDI49
NCBI taxonomy Id: 585423
Other names: S. sp. KORDI-49, Synechococcus sp. KORDI-49
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