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Information on EC 2.7.7.52 - RNA uridylyltransferase and Organism(s) Drosophila melanogaster and UniProt Accession Q9VI58

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.52 RNA uridylyltransferase
IUBMB Comments
The enzyme requires an oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as a primer.
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This record set is specific for:
Drosophila melanogaster
UNIPROT: Q9VI58
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The taxonomic range for the selected organisms is: Drosophila melanogaster
The enzyme appears in selected viruses and cellular organisms
Synonyms
tailor, tutase, zcchc11, terminal uridylyl transferase, heso1, rna editing tutase, terminal uridylyltransferase, meat1, tutase 1, u6-tutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3' terminal uridylyl transferase
-
terminal uridylyl transferase
-
terminal uridylyltransferase Tailor
-
3' terminal uridylyl transferase
-
-
terminal uridylyltransferase
-
-
-
-
TUT
-
-
-
-
uridylyltransferase, terminal
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UTP:RNA uridylyltransferase
The enzyme requires an oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as a primer.
CAS REGISTRY NUMBER
COMMENTARY hide
78519-53-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UTP + 5'-Cy5-GUGGGUAUCUGGGAGAUUACAUAUUCACAG-3'
?
show the reaction diagram
-
-
-
?
UTP + 5-Cy5-CAUAUUCACAG-3'
?
show the reaction diagram
-
-
-
?
UTP + miR-1003 RNAn
diphosphate + miR-1003 RNAn+1
show the reaction diagram
-
-
-
?
UTP + miR-1003-3p-G
?
show the reaction diagram
22-nt single stranded RNA oligonucleotide derived from the miR-1003 stem-loop
-
-
?
UTP + mirtronRNAn
diphosphate + mirtronRNAn+1
show the reaction diagram
the enzyme preferentially catalyzes the uridylation of mirtronRNAs ending in 3'G and 3'U
-
-
?
UTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
UTP + miRNAn
diphosphate + miRNAn+1
show the reaction diagram
-
-
-
-
?
additional information
?
-
the enzyme exhibits significantly higher tailing efficiency for substrates with a 3'-terminal G or U
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UTP + miR-1003 RNAn
diphosphate + miR-1003 RNAn+1
show the reaction diagram
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
UTP + miRNAn
diphosphate + miRNAn+1
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme plays a crucial role as the repressor in the biogenesis pathway of splicing-derived mirtron pre-miRNAs
physiological function
isoform Tailor preferentially uridylates mirtron hairpins, thereby impeding the production of non-canonical microRNAs. Mirtron selectivity is explained by primary sequence specificity of Tailor, selecting substrates ending with a 3'-guanosine. In contrast to mirtrons, conserved Drosophila precursor micro-RNAs are significantly depleted in 3'-guanosine, thereby escaping regulatory uridylation. Cytoplasmic Tailor is required for miRNA uridylation and normal fertility in flies
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TUTT_DROME
560
0
63945
Swiss-Prot
other Location (Reliability: 3)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme bound to uridine-5'-[(alpha,beta)-imido]triphosphate, hanging drop vapor diffusion method, using 20% (v/v) glycerol ethoxylate. Enzyme bound to GpU, sitting drop vapor diffusion method, using 30% (v/v) glycerol ethoxylate and 60 mM sodium malonate, pH 7.0. Enzyme bound to CACAGU, hanging drop vapor diffusion method, using 35% (v/v) glycerol ethoxylate and 75 mM sodium malonate, pH 7.0. Enzyme bound to U6 RNA, sitting drop vapor diffusion method, using 35% (v/v) glycerol ethoxylate and 90 mM sodium malonate, pH 7.0
enzyme residues 202-560 and enzyme in complex with RNA stretches 5 -AGU-3 and 5 -AGUU-3 , sitting drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.4, 50 mM NaCl, 0.2 M lithium sulfate monohydrate and 15% (w/v) PEG3350
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D280A
the mutation abrogates enzyme activity
H294A
the enzymatic activity of the mutant is reduced by about 61% as compared to the wild type enzyme
N347A
the uridylation efficiency of the mutant is reduced dramatically to about 7% when compared with that of wild type enzyme
Q519A
the activity of the mutant is reduced compared to the wild type enzyme. The mutant tails 3'-G, 3'-A and 3'-C substrates with comparable efficiencies
R295A
the enzymatic activity of the mutant is reduced by about 84% as compared to the wild type enzyme
R295K
the enzymatic activity of the mutant is reduced by about 80% as compared to the wild type enzyme
R327A
R327K
V328I
the mutation barely affects the enzyme's binding with RNA substrate and also exhibits a obvious reduction in uridylation efficiency as compared to the wild type enzyme
V328L
the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate
V328R
the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration
Ni-NTA resin column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Gold (DE3) cells
expressed in Sf9 insect cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reimao-Pinto, M.M.; Ignatova, V.; Burkard, T.R.; Hung, J.H.; Manzenreither, R.A.; Sowemimo, I.; Herzog, V.A.; Reichholf, B.; Farina-Lopez, S.; Ameres, S.L.
Uridylation of RNA hairpins by tailor confines the emergence of microRNAs in Drosophila
Mol. Cell
59
203-216
2015
Drosophila melanogaster (Q9VI58)
Manually annotated by BRENDA team
Modepalli, V.; Moran, Y.
Evolution of miRNA tailing by 3' terminal uridylyl transferases in Metazoa
Genome Biol. Evol.
9
1547-1560
2017
Drosophila melanogaster, Hydra vulgaris, Nematostella vectensis, Amphimedon queenslandica
Manually annotated by BRENDA team
Kroupova, A.; Ivascu, A.; Reimao-Pinto, M.M.; Ameres, S.L.; Jinek, M.
Structural basis for acceptor RNA substrate selectivity of the 3 terminal uridylyl transferase Tailor
Nucleic Acids Res.
47
1030-1042
2019
Drosophila melanogaster (Q9VI58)
Manually annotated by BRENDA team
Cheng, L.; Li, F.; Jiang, Y.; Yu, H.; Xie, C.; Shi, Y.; Gong, Q.
Structural insights into a unique preference for 3 terminal guanine of mirtron in Drosophila TUTase Tailor
Nucleic Acids Res.
47
495-508
2019
Drosophila melanogaster (Q9VI58)
Manually annotated by BRENDA team