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TRM44 protein (Saccharomyces cerevisiae) - STRING interaction network
"TRM44" - tRNA(Ser) Um(44) 2'-O-methyltransferase in Saccharomyces cerevisiae
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Known Interactions
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Predicted Interactions
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textmining
co-expression
protein homology
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TRM44tRNA(Ser) Um(44) 2’-O-methyltransferase; involved in maintaining levels of the tRNA-Ser species tS(CGA) and tS(UGA); conserved among metazoans and fungi but there does not appear to be a homolog in plants; TRM44 is a non-essential gene; tRNA (uracil-O(2)-)-methyltransferase, which catalyzes the formation of O(2)-methyluracil at position 44 (Um44) in tRNA(Ser) (567 aa)    
Predicted Functional Partners:
TAN1
Putative tRNA acetyltransferase, RNA-binding protein required for the formation of the modified nucleoside N(4)-acetylcytidine in serine and leucine tRNAs but not required for the same modification in 18S rRNA; Probable tRNA acetyltransferase required for the formation of the modified nucleoside N(4)-acetylcytidine in serine and leucine tRNAs. Binds RNA (289 aa)
       
 
  0.827
TRM8
Noncatalytic subunit of a tRNA methyltransferase complex; Trm8p and Trm82p comprise an enzyme that catalyzes a methyl-transfer from S-adenosyl-l-methionine to the N(7) atom of guanine at position 46 in tRNA; Trm8 lacks catalytic activity if not boun /.../rm82p; Methyltransferase that catalyzes the formation of N(7)- methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity (286 aa)
     
   
  0.735
TRM13
2’-O-methyltransferase responsible for modification of tRNA at position 4; C-terminal domain has similarity to Rossmann-fold (RFM) superfamily of RNA methyltransferases; tRNA methylase which 2’-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His) (476 aa)
     
   
  0.722
NCL1
S-adenosyl-L-methionine-dependent tRNA- m5C-methyltransferase, methylates cytosine to m5C at several positions in tRNAs and intron-containing pre-tRNAs; similar to Nop2p and human proliferation associated nucleolar protein p120; Methylates cytosine to m5C at several positions in different tRNAs and pre-tRNAs containing intron. Able to modify tRNAs at all four positions (34, 40, 48 and 49) at which m5C has been found in tRNAs. May be involved in ribosome biogenesis as its disruption leads to increased sensitivity to the antibiotic paromomycin (684 aa)
     
   
  0.717
MET22
Bisphosphate-3’-nucleotidase, involved in salt tolerance and methionine biogenesis; dephosphorylates 3’-phosphoadenosine-5’-phosphate and 3’-phosphoadenosine-5’-phosphosulfate, intermediates of the sulfate assimilation pathway; Converts adenosine 3’-phosphate 5’-phosphosulfate (PAPS) to adenosine 5’-phosphosulfate (APS) and 3’(2’)-phosphoadenosine 5’- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. Involved in salt tolerance. Confers resistance to lithium (357 aa)
       
 
  0.687
TRM2
tRNA methyltransferase, 5-methylates the uridine residue at position 54 of tRNAs and may also have a role in tRNA stabilization or maturation; endo-exonuclease with a role in DNA repair; Catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNA. May also have a role in tRNA stabilization or maturation (639 aa)
     
   
  0.660
RRP9
Protein involved in pre-rRNA processing, associated with U3 snRNP; component of small ribosomal subunit (SSU) processosome; ortholog of the human U3-55k protein; Involved in nucleolar processing of pre-18S ribosomal RNA. Required for efficient pre-rRNA cleavage at sites A0, A1 and A2, and biosynthesis of 18S rRNA (573 aa)
     
        0.625
PAP2
Non-canonical poly(A) polymerase, involved in nuclear RNA degradation as a component of the TRAMP complex; catalyzes polyadenylation of hypomodified tRNAs, and snoRNA and rRNA precursors; overlapping but non-redundant functions with Trf5p; Catalytic subunit of the TRAMP complex which has a poly(A) RNA polymerase activity and is involved in a post- transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts gene [...] (584 aa)
     
 
  0.621
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)
     
   
  0.588
BUD17
Putative pyridoxal kinase, a key enzyme in vitamin B6 metabolism; involved in bud-site selection; diploid mutants display a random rather than a bipolar budding pattern; similarity to yeast BUD16 and human pyridoxal kinase (PDXK); Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection (317 aa)
           
  0.578
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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