UniProt functional annotation for Q8WQX5



	UniProt functional annotation for Q8WQX5

UniProt code: Q8WQX5.

Organism: Trypanosoma brucei brucei.

Taxonomy: Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; Trypanosomatida; Trypanosomatidae; Trypanosoma.

Function: Terminal uridylyltransferase which is involved in the post- transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-RNA (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351). Specifically, catalyzes the addition of Us to the 3'-hydroxyl group of guided RNA (gRNA), ribosomal RNA (rRNA) and some mRNAs (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351). As part of the mitochondrial 3' processome (MPsome), catalyzes the primary 3' uridylation of gRNA precursors to facilitate their recognition and to induce their processive 3'-5' degradation by DSS1, and the secondary 3' uridylation of mature gRNAs (PubMed:26833087). Involved in the 3' uridylylation of the long A/U tail of some edited and never-edited mRNAs (PubMed:20086102). Promotes 3' uridylylation- mediated decay of some never-edited mRNAs (PubMed:20086102). Does not mediate RNA-independent UTP polymerization (PubMed:27744351). {ECO:0000269|PubMed:11893335, ECO:0000269|PubMed:20086102, ECO:0000269|PubMed:26833087, ECO:0000269|PubMed:27744351}.

Catalytic activity: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:11128, Rhea:RHEA-COMP:14648, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:83400, ChEBI:CHEBI:140627; EC=2.7.7.52; Evidence={ECO:0000269|PubMed:11893335, ECO:0000269|PubMed:15304317, ECO:0000269|PubMed:19465686, ECO:0000269|PubMed:26833087, ECO:0000269|PubMed:27744351, ECO:0000305|PubMed:20086102};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15304317, ECO:0000305|PubMed:27744351}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8WQX6}; Note=Binds 1 Mg(2+) or Mn(2+) per subunit (PubMed:27744351). The type of divalent cation used by the enzyme affects the nucleotide specificity; Mg(2+) induces predominantly uridine (U) incorporation while Mn(2+) induces also substantial incorporation of both adenine (A) and cytosine (C) (By similarity). {ECO:0000250|UniProtKB:Q8WQX6, ECO:0000269|PubMed:27744351};

Biophysicochemical properties: Kinetic parameters: KM=17 uM for UTP (with 6(U) single-stranded RNA as substrate) {ECO:0000269|PubMed:19465686}; KM=1.5 uM for UTP (with double-stranded RNA as substrate) {ECO:0000269|PubMed:19465686}; KM=8.5 uM for UTP (at 27 degrees Celsius) {ECO:0000269|PubMed:27744351}; KM=0.53 uM for RNA (at 27 degrees Celsius) {ECO:0000269|PubMed:27744351}; Note=KM is 18-28 mM for UTP (at 27 degrees Celsius and 12 (U) single- stranded RNA as substrate) (PubMed:15304317). kcat is 100 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.0012 min(-1) with UTP and double- stranded RNA as substrates (PubMed:19465686). kcat is 15.5 min(-1) with UTP as substrate (PubMed:27744351). kcat is 23.5 min(-1) with RNA as substrate (PubMed:27744351). {ECO:0000269|PubMed:15304317, ECO:0000269|PubMed:19465686, ECO:0000269|PubMed:27744351};

Subunit: Oligomer (PubMed:27744351). Component of the mitochondrial 3' processome (MPsome) complex composed at least of terminal uridylyltransferase KRET1/TUT1, 3'-5' exonuclease DSS1, MPSS1, MPSS2 and MPSS3 (PubMed:26833087, PubMed:27744351). Within the complex, interacts with DSS1, MPSS1 and MPSS3 (PubMed:26833087). {ECO:0000269|PubMed:26833087, ECO:0000269|PubMed:27744351}.

Subcellular location: Mitochondrion {ECO:0000269|PubMed:19465686, ECO:0000269|PubMed:26833087, ECO:0000269|PubMed:27744351}.

Developmental stage: Expressed at the procyclic stage (at protein level). {ECO:0000269|PubMed:26833087, ECO:0000269|PubMed:27744351}.

Domain: The C2H2-type zinc finger domain is required for the proper folding of the catalytic domain, but is dispensable for uridylation of single strand RNA substrate. {ECO:0000269|PubMed:27744351}.

Disruption phenotype: RNAi-mediated knockdown at the procyclic stage causes severe growth defect and a severe reduction in mRNA editing (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351). Reduced production of guided RNAs (gRNA) and rRNAs due to a block in the processing of gRNA and rRNA precursors (PubMed:20086102, PubMed:26833087). Accumulation of unprocessed precursors for some pre- edited and never-edited mRNAs (PubMed:20086102). {ECO:0000269|PubMed:11893335, ECO:0000269|PubMed:20086102, ECO:0000269|PubMed:26833087, ECO:0000269|PubMed:27744351}.

Similarity: Belongs to the DNA polymerase type-B-like family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Trypanosoma brucei brucei.
Taxonomy:		Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; Trypanosomatida; Trypanosomatidae; Trypanosoma.



Function:		Terminal uridylyltransferase which is involved in the post- transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-RNA (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351). Specifically, catalyzes the addition of Us to the 3'-hydroxyl group of guided RNA (gRNA), ribosomal RNA (rRNA) and some mRNAs (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351). As part of the mitochondrial 3' processome (MPsome), catalyzes the primary 3' uridylation of gRNA precursors to facilitate their recognition and to induce their processive 3'-5' degradation by DSS1, and the secondary 3' uridylation of mature gRNAs (PubMed:26833087). Involved in the 3' uridylylation of the long A/U tail of some edited and never-edited mRNAs (PubMed:20086102). Promotes 3' uridylylation- mediated decay of some never-edited mRNAs (PubMed:20086102). Does not mediate RNA-independent UTP polymerization (PubMed:27744351). {ECO:0000269\|PubMed:11893335, ECO:0000269\|PubMed:20086102, ECO:0000269\|PubMed:26833087, ECO:0000269\|PubMed:27744351}.


Catalytic activity:		Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:11128, Rhea:RHEA-COMP:14648, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:83400, ChEBI:CHEBI:140627; EC=2.7.7.52; Evidence={ECO:0000269\|PubMed:11893335, ECO:0000269\|PubMed:15304317, ECO:0000269\|PubMed:19465686, ECO:0000269\|PubMed:26833087, ECO:0000269\|PubMed:27744351, ECO:0000305\|PubMed:20086102};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:15304317, ECO:0000305\|PubMed:27744351}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250\|UniProtKB:Q8WQX6}; Note=Binds 1 Mg(2+) or Mn(2+) per subunit (PubMed:27744351). The type of divalent cation used by the enzyme affects the nucleotide specificity; Mg(2+) induces predominantly uridine (U) incorporation while Mn(2+) induces also substantial incorporation of both adenine (A) and cytosine (C) (By similarity). {ECO:0000250\|UniProtKB:Q8WQX6, ECO:0000269\|PubMed:27744351};
Biophysicochemical properties:		Kinetic parameters: KM=17 uM for UTP (with 6(U) single-stranded RNA as substrate) {ECO:0000269\|PubMed:19465686}; KM=1.5 uM for UTP (with double-stranded RNA as substrate) {ECO:0000269\|PubMed:19465686}; KM=8.5 uM for UTP (at 27 degrees Celsius) {ECO:0000269\|PubMed:27744351}; KM=0.53 uM for RNA (at 27 degrees Celsius) {ECO:0000269\|PubMed:27744351}; Note=KM is 18-28 mM for UTP (at 27 degrees Celsius and 12 (U) single- stranded RNA as substrate) (PubMed:15304317). kcat is 100 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.0012 min(-1) with UTP and double- stranded RNA as substrates (PubMed:19465686). kcat is 15.5 min(-1) with UTP as substrate (PubMed:27744351). kcat is 23.5 min(-1) with RNA as substrate (PubMed:27744351). {ECO:0000269\|PubMed:15304317, ECO:0000269\|PubMed:19465686, ECO:0000269\|PubMed:27744351};
Subunit:		Oligomer (PubMed:27744351). Component of the mitochondrial 3' processome (MPsome) complex composed at least of terminal uridylyltransferase KRET1/TUT1, 3'-5' exonuclease DSS1, MPSS1, MPSS2 and MPSS3 (PubMed:26833087, PubMed:27744351). Within the complex, interacts with DSS1, MPSS1 and MPSS3 (PubMed:26833087). {ECO:0000269\|PubMed:26833087, ECO:0000269\|PubMed:27744351}.
Subcellular location:		Mitochondrion {ECO:0000269\|PubMed:19465686, ECO:0000269\|PubMed:26833087, ECO:0000269\|PubMed:27744351}.
Developmental stage:		Expressed at the procyclic stage (at protein level). {ECO:0000269\|PubMed:26833087, ECO:0000269\|PubMed:27744351}.
Domain:		The C2H2-type zinc finger domain is required for the proper folding of the catalytic domain, but is dispensable for uridylation of single strand RNA substrate. {ECO:0000269\|PubMed:27744351}.
Disruption phenotype:		RNAi-mediated knockdown at the procyclic stage causes severe growth defect and a severe reduction in mRNA editing (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351). Reduced production of guided RNAs (gRNA) and rRNAs due to a block in the processing of gRNA and rRNA precursors (PubMed:20086102, PubMed:26833087). Accumulation of unprocessed precursors for some pre- edited and never-edited mRNAs (PubMed:20086102). {ECO:0000269\|PubMed:11893335, ECO:0000269\|PubMed:20086102, ECO:0000269\|PubMed:26833087, ECO:0000269\|PubMed:27744351}.
Similarity:		Belongs to the DNA polymerase type-B-like family. {ECO:0000305}.