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TAD1 protein (Saccharomyces cerevisiae) - STRING interaction network
"TAD1" - tRNA-specific adenosine deaminase, deaminates adenosine-37 to inosine in tRNA-Ala in Saccharomyces cerevisiae
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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TAD1tRNA-specific adenosine deaminase, deaminates adenosine-37 to inosine in tRNA-Ala; Deaminates adenosine-37 to inosine in tRNA-Ala (400 aa)    
Predicted Functional Partners:
TAD2
Subunit of tRNA-specific adenosine-34 deaminase, forms a heterodimer with Tad3p that converts adenosine to inosine at the wobble position of several tRNAs; Deaminates adenosine-34 to inosine in many tRNAs (250 aa)
       
 
  0.928
PRE6
Alpha 4 subunit of the 20S proteasome; may replace alpha 3 subunit (Pre9p) under stress conditions to create a more active proteasomal isoform; GFP-fusion protein relocates from cytosol to the mitochondrial surface upon oxidative stress; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving [...] (254 aa)
       
      0.827
PRE8
Alpha 2 subunit of the 20S proteasome; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity (250 aa)
       
      0.827
SCL1
Alpha 1 subunit of the 20S proteasome involved in the degradation of ubiquitinated substrates; 20S proteasome is the core complex of the 26S proteasome; essential for growth; detected in the mitochondria; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basi [...] (252 aa)
       
      0.827
TAD3
Subunit of tRNA-specific adenosine-34 deaminase, forms a heterodimer with Tad2p that converts adenosine to inosine at the wobble position of several tRNAs; Deaminates adenosine-34 to inosine in many tRNAs (322 aa)
           
  0.716
YDR048C
Dubious ORF unlikely to encode a functional protein, based on available experimental and comparative sequence data (104 aa)
           
  0.636
CDD1
Cytidine deaminase; catalyzes the modification of cytidine to uridine in vitro but native RNA substrates have not been identified, localizes to both the nucleus and cytoplasm; This enzyme scavenges exogenous and endogenous cytidine and 2’-deoxycytidine for UMP synthesis (142 aa)
           
  0.600
TRM5
tRNA(m(1)G37)methyltransferase, methylates a tRNA base adjacent to the anticodon that has a role in prevention of frameshifting; highly conserved across Archaea, Bacteria, and Eukarya; Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5’ of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding. Postspliced cytoplasmic tRNAs are imported into the nucleus, wh [...] (499 aa)
           
  0.580
TRM7
2’-O-ribose methyltransferase, methylates the 2’-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop; Methylates the 2’-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of tRNA(Phe), tRNA(Trp) and tRNA(Leu(UAA)). Requires TRM732 for methylation of the cytidine at position 32 and RTT10/TRM734 for methylation of the nucleotides at position 34 in substrate tRNAs. Lack of either of these modifications in tRNA(Phe) reduces formation of wybutosine from 1- methylguanosine at position 37 (310 aa)
           
  0.489
TRM1
tRNA methyltransferase; two forms of the protein are made by alternative translation starts; localizes to both the nucleus and mitochondrion to produce the modified base N2,N2-dimethylguanosine in tRNAs in both compartments; Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. Required for the modification of both mitochondrial and cytoplasmic tRNAs (570 aa)
           
  0.480
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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