STRINGSTRING
fusA fusA SDM73401.1 SDM73401.1 SDM95782.1 SDM95782.1 SDM96408.1 SDM96408.1 serS serS SDN05225.1 SDN05225.1 metG metG aspS aspS SDN20350.1 SDN20350.1 metG-2 metG-2 SDN22024.1 SDN22024.1 SDN47707.1 SDN47707.1 SDN51679.1 SDN51679.1 ileS ileS SDN72675.1 SDN72675.1 tyrS tyrS SDN94722.1 SDN94722.1 SDN96385.1 SDN96385.1 SDN97258.1 SDN97258.1 valS valS leuS leuS glyQS glyQS fusA-2 fusA-2 serS-2 serS-2 SDO37412.1 SDO37412.1 argS argS lysS lysS trpS trpS pheT pheT pheS pheS mshC mshC SDO61312.1 SDO61312.1 thrS thrS hisS hisS SDO86390.1 SDO86390.1 SDP01751.1 SDP01751.1 proS proS alaS alaS fmt fmt cysS cysS gatB gatB gatA gatA gatC gatC gltX gltX trpS-2 trpS-2
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:
fusAElongation factor 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. (708 aa)
SDM73401.1Ribosomal protection tetracycline resistance protein. (672 aa)
SDM95782.1methionyl-tRNA formyltransferase. (289 aa)
SDM96408.1L-seryl-tRNA(Sec) selenium transferase. (388 aa)
serSseryl-tRNA synthetase; 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). (428 aa)
SDN05225.1prolyl-tRNA synthetase. (188 aa)
metGmethionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (578 aa)
aspSaspartyl-tRNA synthetase; 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)
SDN20350.1Arginyl tRNA synthetase N terminal domain-containing protein. (554 aa)
metG-2methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (540 aa)
SDN22024.1lysyl-tRNA synthetase, class 2. (806 aa)
SDN47707.1tRNA synthetase class II core domain (G, H, P, S and T). (280 aa)
SDN51679.1tRNA synthetases class II (A). (400 aa)
ileSIsoleucyl-tRNA synthetase; 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. (1048 aa)
SDN72675.1Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase; Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. (174 aa)
tyrStyrosyl-tRNA synthetase; 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. (424 aa)
SDN94722.1lysyl-tRNA synthetase, class 2. (601 aa)
SDN96385.1Ser-tRNA(Ala) deacylase AlaX (editing enzyme). (225 aa)
SDN97258.1methionyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (515 aa)
valSvalyl-tRNA synthetase; 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. (938 aa)
leuSleucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (964 aa)
glyQSglycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (460 aa)
fusA-2Translation elongation factor 2 (EF-2/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. [...] (708 aa)
serS-2seryl-tRNA synthetase; 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). (433 aa)
SDO37412.1Uncharacterized conserved protein. (334 aa)
argSarginyl-tRNA synthetase. (591 aa)
lysSlysyl-tRNA synthetase, class I; Belongs to the class-I aminoacyl-tRNA synthetase family. (580 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (337 aa)
pheTphenylalanyl-tRNA synthetase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (835 aa)
pheSphenylalanyl-tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (373 aa)
mshCL-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Catalyzes the ATP-dependent condensation of GlcN-Ins and L- cysteine to form L-Cys-GlcN-Ins; Belongs to the class-I aminoacyl-tRNA synthetase family. MshC subfamily. (380 aa)
SDO61312.1Translation elongation factor 2 (EF-2/EF-G). (743 aa)
thrSthreonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (660 aa)
hisShistidyl-tRNA synthetase. (423 aa)
SDO86390.1Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC. (179 aa)
SDP01751.1Hypothetical protein. (253 aa)
proSprolyl-tRNA synthetase; 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). (470 aa)
alaSalanyl-tRNA synthetase; 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. (889 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. (310 aa)
cysScysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (463 aa)
gatBaspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. (500 aa)
gatAaspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). (497 aa)
gatCaspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. (99 aa)
gltXglutamyl-tRNA synthetase; 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). (499 aa)
trpS-2tryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (335 aa)
Your Current Organism:
Streptomyces guanduensis
NCBI taxonomy Id: 310781
Other names: CGMCC 4.2022, JCM 13274, NBRC 102070, S. guanduensis, Streptomyces guanduensis Xu et al. 2006, Streptomyces sp. 701, strain 701
Server load: low (38%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.