STRINGSTRING
metG_4 metG_4 lysS lysS argS_3 argS_3 tyrS tyrS leuS leuS pheS pheS pheT_2 pheT_2 ileS_2 ileS_2 metG_2 metG_2 argS_1 argS_1 proS proS ileS_1 ileS_1 argS_2 argS_2 gltX gltX
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:
metG_4Unannotated protein; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (651 aa)
lysSUnannotated protein; Belongs to the class-II aminoacyl-tRNA synthetase family. (494 aa)
argS_3Unannotated protein. (555 aa)
tyrSUnannotated protein; 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. (418 aa)
leuSUnannotated protein; Belongs to the class-I aminoacyl-tRNA synthetase family. (804 aa)
pheSUnannotated protein; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (401 aa)
pheT_2Unannotated protein; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (809 aa)
ileS_2Unannotated protein; 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. (918 aa)
metG_2Unannotated protein; Belongs to the class-I aminoacyl-tRNA synthetase family. (559 aa)
argS_1Unannotated protein. (555 aa)
proSUnannotated protein; 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). (479 aa)
ileS_1Unannotated protein; 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. (1026 aa)
argS_2Unannotated protein. (554 aa)
gltXUnannotated protein; 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. (489 aa)
Your Current Organism:
Virgibacillus dokdonensis
NCBI taxonomy Id: 302167
Other names: DSM 16826, KCTC 3933, Ornithinibacillus sp. NY-1, Ornithinibacillus sp. NY-11, Ornithinibacillus sp. NY-6, V. dokdonensis, Virgibacillus dokdonensis Yoon et al. 2005, strain DSW-10
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