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trmD trmD trmL trmL trmI trmI trmJ trmJ trmN trmN ygeR ygeR mutT mutT phoA phoA thiI thiI cdd cdd yfaE yfaE
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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trmDtRNA m(1)G37 methyltransferase, SAM-dependent; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. (255 aa)
trmLtRNA Leu mC34,mU34 2'-O-methyltransferase, SAM-dependent; Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide. Recognition of the target requires a pyridine at position 34 and N(6)-(isopentenyl)-2-methylthioadenosine at position 37. (157 aa)
trmItRNA m(7)G46 methyltransferase, SAM-dependent; Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family. (239 aa)
trmJtRNA mC32,mU32 2'-O-methyltransferase, SAM-dependent; Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. Can also methylate adenosine or guanosine, even though these nucleosides are rare or absent at position 32 in the anticodon loop of tRNA. (246 aa)
trmNtRNA1(Val) (adenine(37)-N6)-methyltransferase; Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC); Belongs to the methyltransferase superfamily. tRNA (adenine-N(6)-)-methyltransferase family. (245 aa)
ygeRtRNA-Gly; Anticodon: CCC; Belongs to the peptidase M23B family. (251 aa)
mutTdGTP-preferring nucleoside triphosphate pyrophosphohydrolase; Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo-dGTP to the monophosphate; Belongs to the Nudix hydrolase family. (129 aa)
phoAAlkaline phosphatase; start codon corrected; Protein involved in phosphorus metabolic process; Belongs to the alkaline phosphatase family. (471 aa)
thiItRNA s(4)U8 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. Belongs to the ThiI family. (482 aa)
cddCytidine/deoxycytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. (294 aa)
yfaEUncharacterized ferredoxin-like protein YfaE; Ferredoxin involved with ribonucleotide reductase diferric-tyrosyl radical (Y*) cofactor maintenance. (84 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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