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glnS glnS gltX gltX ileS ileS serS serS pheS pheS hisS hisS cysS cysS thrS thrS pheT pheT valS valS proS proS argS argS lysS lysS alaS alaS aspS aspS metG metG asnS asnS leuS leuS KQS_13475 KQS_13475 tyrS tyrS trpS trpS
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:
glnSGlutamine--tRNA ligase. (560 aa)
gltXGlutamate--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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (500 aa)
ileSIsoleucine--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. (1154 aa)
serSSerine--tRNA ligase. (423 aa)
pheSPhenylalanine--tRNA ligase alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (339 aa)
hisSHistidine--tRNA ligase. (456 aa)
cysSCysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. (493 aa)
thrSThreonine--tRNA ligase; 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). (646 aa)
pheTPhenylalanine--tRNA ligase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (810 aa)
valSValine--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. (875 aa)
proSProline--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). (492 aa)
argSArginine--tRNA ligase. (593 aa)
lysSLysine--tRNA ligase; Belongs to the class-II aminoacyl-tRNA synthetase family. (563 aa)
alaSAlanine--tRNA ligase; 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. (878 aa)
aspSAspartate--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. (582 aa)
metGMethionine--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. (685 aa)
asnSAsparagine--tRNA ligase. (478 aa)
leuSLeucine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. (1002 aa)
KQS_13475Putative efflux transporter, RND superfamily. (809 aa)
tyrSTyrosine--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. (434 aa)
trpSTryptophan--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. (322 aa)
Your Current Organism:
Flavobacterium indicum
NCBI taxonomy Id: 1094466
Other names: F. indicum GPTSA100-9 = DSM 17447, Flavobacterium indicum CIP 109464, Flavobacterium indicum DSM 17447, Flavobacterium indicum DSM 17447 = GPTSA100-9, Flavobacterium indicum GPTSA100-9, Flavobacterium indicum GPTSA100-9 = DSM 17447, Flavobacterium sp. GPTSA100-9
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