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hisS hisS thrS thrS pheT pheT pheS pheS tyrS tyrS ileS ileS leuS leuS valS valS aspS aspS metG metG metG-2 metG-2 argS argS AGS71828.1 AGS71828.1 gltX gltX proS proS AGS73103.1 AGS73103.1 lysS lysS
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
hisSCOG0124 Histidyl-tRNA synthetase. (420 aa)
thrSCOG0441 Threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (658 aa)
pheTphenylalanyl-tRNA ligase subunit beta; COG0073 EMAP domain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (840 aa)
pheSCOG0016 Phenylalanyl-tRNA synthetase alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (373 aa)
tyrStyrosyl-tRNA ligase; 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. (422 aa)
ileSisoleucyl-tRNA ligase; 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. (1047 aa)
leuSCOG0495 Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (960 aa)
valSvalyl-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. (876 aa)
aspSaspartyl-tRNA ligase; 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. (587 aa)
metGmethionyl-tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (532 aa)
metG-2methionyl-tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (571 aa)
argSCOG0018 Arginyl-tRNA synthetase. (589 aa)
AGS71828.1COG0018 Arginyl-tRNA synthetase. (482 aa)
gltXglutamyl-tRNA ligase; 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). (475 aa)
proSprolyl-tRNA ligase; 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 deacyla [...] (567 aa)
AGS73103.1COG0143 Methionyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (543 aa)
lysSlysyl-tRNA ligase; Belongs to the class-II aminoacyl-tRNA synthetase family. (1092 aa)
Your Current Organism:
Streptomyces collinus
NCBI taxonomy Id: 1214242
Other names: S. collinus Tu 365, Streptomyces collinus Tu 365
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