STRINGSTRING
metG metG serS serS pheS pheS tyrS tyrS ileS ileS aspS aspS FP0384 FP0384 csaA csaA cysS cysS thrS thrS pheT pheT lysS lysS fusA fusA proS proS argS argS valS valS alaS alaS fmt fmt hisS hisS trpS trpS asnS asnS leuS leuS glyS glyS glnS glnS 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:
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. (686 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)
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. (431 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. (1133 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. (583 aa)
FP0384Protein of unknown function. (121 aa)
csaAProtein secretion chaperone CsaA. (112 aa)
cysSCysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. (495 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). Also edits incorrectly charged L-seryl-tRNA(Thr). (648 aa)
pheTPhenylalanine--tRNA ligase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (806 aa)
lysSLysine--tRNA ligase; Belongs to the class-II aminoacyl-tRNA synthetase family. (563 aa)
fusAElongation factor G (EF-G); Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. (718 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. (601 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)
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. (887 aa)
fmtMethionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. (316 aa)
hisSHistidine--tRNA ligase. (472 aa)
trpSTryptophan--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. (324 aa)
asnSAsparagine--tRNA ligase. (478 aa)
leuSLeucine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. (962 aa)
glySGlycine--tRNA ligase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (513 aa)
glnSGlutamine--tRNA ligase. (695 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. (501 aa)
Your Current Organism:
Flavobacterium psychrophilum
NCBI taxonomy Id: 402612
Other names: F. psychrophilum JIP02/86, Flavobacterium psychrophilum JIP02/86, Flavobacterium psychrophilum str. JIP02/86, Flavobacterium psychrophilum strain JIP02/86
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