STRINGSTRING
lysS lysS alaS alaS prfC prfC tuf tuf argS argS infA infA fusA fusA tyrS tyrS glyQS glyQS leuS leuS greA greA ileS ileS metG metG AJR02830.1 AJR02830.1 gltX gltX AJR02899.1 AJR02899.1 pheS pheS lepA lepA aspS aspS asnS asnS frr frr tsf tsf nusA nusA infB infB AJR03153.1 AJR03153.1 cysS cysS proS proS valS valS gatB gatB hisS hisS fmt fmt AJR04205.1 AJR04205.1 efp efp prfB prfB pheT pheT thrS thrS AJR04591.1 AJR04591.1 def def prfA prfA
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:
lysSlysyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family. (562 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. (870 aa)
prfCPeptide chain release factor 3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily. (529 aa)
tufElongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (395 aa)
argSarginyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology. (591 aa)
infATranslation initiation factor IF-1; One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. (71 aa)
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)
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. (431 aa)
glyQSglycyl-tRNA synthetease; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (513 aa)
leuSleucyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family. (996 aa)
greATranscription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. (157 aa)
ileSisoleucyl-tRNA synthase; 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. (1134 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. (688 aa)
AJR02830.1tryptophanyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family. (322 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (502 aa)
AJR02899.1glutaminyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology. (666 aa)
pheSphenylalanyl-tRNA synthetase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (339 aa)
lepAElongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. (598 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. (584 aa)
asnSasparaginyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology. (477 aa)
frrRibosome-recycling factor; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another; Belongs to the RRF family. (185 aa)
tsfElongation factor Ts; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family. (324 aa)
nusATranscription elongation factor NusA; Participates in both transcription termination and antitermination. (410 aa)
infBTranslation initiation factor IF-2; One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily. (940 aa)
AJR03153.1Translation initiation factor IF-2; Derived by automated computational analysis using gene prediction method: Protein Homology. (129 aa)
cysScysteine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family. (493 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)
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. (878 aa)
gatBaspartyl-tRNA synthetase; 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. (1112 aa)
hisShistidyl-tRNA synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (457 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. (315 aa)
AJR04205.1Translation initiation factor SUI1-related protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (110 aa)
efpElongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. (188 aa)
prfBPeptide chain release factor 2; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. (317 aa)
pheTphenylalanyl-tRNA synthetase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (808 aa)
thrSthreonyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family. (644 aa)
AJR04591.1Translation initiation factor IF-3; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IF-3 family. (110 aa)
defPeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. (196 aa)
prfAPeptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. (358 aa)
Your Current Organism:
Siansivirga zeaxanthinifaciens
NCBI taxonomy Id: 1454006
Other names: S. zeaxanthinifaciens CC-SAMT-1, Siansivirga zeaxanthinifaciens CC-SAMT-1
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