STRINGSTRING
cysS cysS serS serS gltX gltX aspS aspS tyrS tyrS valS valS ybaK ybaK hisS hisS fusA fusA fmt fmt trpS trpS selA selA proS proS alaS alaS leuS leuS glyS glyS glyQ glyQ lysS lysS metG metG asnS asnS pheS pheS pheT pheT glnS glnS thrS thrS argS argS
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:
cysScysteinyl-tRNA synthetase (cysS); Similar to GB:M59381 SP:P21888 GB:X56234 GB:X59293 PID:145692 percent identity: 75.65; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family. (459 aa)
serSseryl-tRNA synthetase (serS); Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). (429 aa)
gltXglutamyl-tRNA synthetase (gltX); 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). (480 aa)
aspSaspartyl-tRNA synthetase (aspS); 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. (588 aa)
tyrSTyrosyl tRNA synthetase (tyrS); 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. (401 aa)
valSvalyl-tRNA synthetase (valS); 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. (954 aa)
ybaKTranscriptional regulator, putative; Functions in trans to edit the amino acid from incorrectly charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase activity. Probably compensates for the lack of Cys-tRNA(Pro) editing by ProRS. Is also able to deacylate Cys-tRNA(Cys), and displays weak deacylase activity in vitro against Gly-tRNA(Gly), as well as, at higher concentrations, some other correctly charged tRNAs. Does not cleave Pro-tRNA(Pro). Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. (158 aa)
hisShistidyl-tRNA synthetase (hisS); Similar to GB:M11843 SP:P04804 PID:146372 GB:U00096 PID:1788861 percent identity: 66.82; identified by sequence similarity; putative. (423 aa)
fusAElongation factor G (fusA); 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 (By similarity); Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. [...] (700 aa)
fmtmethionyl-tRNA formyltransferase (fmt); 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. (318 aa)
trpStryptophanyl-tRNA synthetase (trpS); Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (334 aa)
selAL-seryl-tRNA selenium transferase (selA); Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (461 aa)
proSprolyl-tRNA synthetase (proS); 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 invol [...] (572 aa)
alaSalanyl-tRNA synthetase (alaS); 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. (874 aa)
leuSleucyl-tRNA synthetase (leuS); Similar to SP:P07813 GB:X06331 PID:41916 GB:U00096 PID:1651269 percent identity: 72.64; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family. (861 aa)
glySglycyl-tRNA synthetase, beta chain (glyS); Similar to SP:P00961 GB:J01622 PID:146223 PID:466697 GB:U00096 percent identity: 69.67; identified by sequence similarity; putative. (688 aa)
glyQglycyl-tRNA synthetase, alpha chain (glyQ); Similar to SP:P00960 GB:J01622 PID:146222 PID:146225 PID:466698 percent identity: 90.64; identified by sequence similarity; putative. (302 aa)
lysSlysyl-tRNA synthetase (lysU); Similar to GB:U14003 GB:J03795 SP:P13030 SP:P14825 GB:M30630 percent identity: 70.38; identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family. (502 aa)
metGmethionyl-tRNA synthetase (metG); Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (682 aa)
asnSasparaginyl-tRNA synthetase (asnS); Similar to GB:M33145 SP:P17242 GB:X68192 PID:147935 PID:41000 percent identity: 80.65; identified by sequence similarity; putative. (477 aa)
pheSphenylalanyl-tRNA synthetase, alpha subunit (pheS); Similar to GB:V00291 SP:P08312 PID:146345 PID:43070 GB:U00096 percent identity: 75.00; identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (329 aa)
pheTphenylalanyl-tRNA synthetase, beta subunit (pheT); Similar to GB:K02844 SP:P07395 PID:146346 PID:43071 GB:U00096 percent identity: 65.28; identified by sequence similarity; putative; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (795 aa)
glnSglutaminyl-tRNA synthetase (glnS); Similar to GB:V01575 SP:P00962 GB:J01617 GB:M10187 PID:146168 percent identity: 76.28; identified by sequence similarity; putative. (557 aa)
thrSthreonyl-tRNA synthetase (thrS); 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). (643 aa)
argSarginyl-tRNA synthetase (argS); Similar to SP:P11875 GB:X15320 PID:581040 GB:U00096 PID:1736522 percent identity: 71.40; identified by sequence similarity; putative. (577 aa)
Your Current Organism:
Haemophilus influenzae
NCBI taxonomy Id: 71421
Other names: H. influenzae Rd KW20, Haemophilus influenzae KW20, Haemophilus influenzae Rd, Haemophilus influenzae Rd KW20
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