STRINGSTRING
cysS cysS etfB etfB etfA etfA argS argS AEE91824.1 AEE91824.1 guaA guaA tyrS tyrS metG metG AEE90596.1 AEE90596.1 tilS tilS AEE92403.1 AEE92403.1 ileS ileS AEE90797.1 AEE90797.1 mnmA mnmA nadE nadE AEE91420.1 AEE91420.1 trpS trpS tmcAL tmcAL coaD coaD valS valS leuS leuS nadD nadD thiI thiI gltX gltX
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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.
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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
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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:
cysSSMART: Cysteinyl-tRNA synthetase, class Ia, DALR; TIGRFAM: Cysteinyl-tRNA synthetase, class Ia; KEGG: toc:Toce_2114 cysteinyl-tRNA synthetase; PFAM: Cysteinyl-tRNA synthetase, class Ia; Cysteinyl-tRNA synthetase, class Ia, DALR; Belongs to the class-I aminoacyl-tRNA synthetase family. (466 aa)
etfBKEGG: ttm:Tthe_1665 electron transfer flavoprotein alpha/beta-subunit; PFAM: Electron transfer flavoprotein, alpha/beta-subunit, N-terminal; SMART: Electron transfer flavoprotein, alpha/beta-subunit, N-terminal. (264 aa)
etfAKEGG: ttm:Tthe_1664 electron transfer flavoprotein alpha subunit; PFAM: Electron transfer flavoprotein, alpha subunit, C-terminal; Electron transfer flavoprotein, alpha/beta-subunit, N-terminal; SMART: Electron transfer flavoprotein, alpha/beta-subunit, N-terminal. (331 aa)
argSKEGG: toc:Toce_2184 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic. (569 aa)
AEE91824.1KEGG: toc:Toce_0386 PP-loop domain protein; TIGRFAM: Conserved hypothetical protein CHP00268; PFAM: tRNA(Ile)-lysidine/2-thiocytidine synthase. (277 aa)
guaAGMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. (511 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. (409 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. (650 aa)
AEE90596.1PFAM: Domain of unknown function DUF218; KEGG: cth:Cthe_1772 hypothetical protein. (193 aa)
tilStRNA(Ile)-lysidine synthase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family. (462 aa)
AEE92403.1Citrate lyase ligase; Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'- dephosphocoenzyme-A) of the gamma subunit of citrate lyase. (343 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. (1045 aa)
AEE90797.1KEGG: toc:Toce_1762 UspA domain protein. (137 aa)
mnmAtRNA-specific 2-thiouridylase mnmA; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. (366 aa)
nadENH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source; Belongs to the NAD synthetase family. (241 aa)
AEE91420.1Riboflavin biosynthesis protein RibF; SMART: Riboflavin kinase; TIGRFAM: Riboflavin kinase/FAD synthetase; KEGG: toc:Toce_1233 riboflavin biosynthesis protein RibF; PFAM: FAD synthetase; Riboflavin kinase. (308 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (327 aa)
tmcALUPF0348 protein; Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac- AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. (419 aa)
coaDPhosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. (160 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. (883 aa)
leuSTIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: toc:Toce_0772 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (816 aa)
nadDNicotinate-nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). (204 aa)
thiItRNA sulfurtransferase; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. (387 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. (491 aa)
Your Current Organism:
Tepidanaerobacter acetatoxydans
NCBI taxonomy Id: 1209989
Other names: T. acetatoxydans Re1, Tepidanaerobacter acetatoxydans Re1, Tepidanaerobacter acetatoxydans str. Re1, Tepidanaerobacter acetatoxydans strain Re1, Tepidanaerobacter sp. Re1
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