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protein coding gene - pct1 (SPAC644.04) - RNA 5'-triphosphatase

Gene summary

Standard name
pct1
Systematic ID
SPAC644.04
Product
RNA 5'-triphosphatase
Organism
Schizosaccharomyces pombe (fission yeast)
UniProt ID
Q9P6Q6
ORFeome ID
13/13F11
Characterisation status
biological role published
Feature type
mRNA gene
Genomic location
chromosome I: 2677086..2679291 forward strand

Annotation

Complementation

PBO:0015228 - does not functionally complement S. cerevisiae CET1

References:

PBO:0091403 - functionally complements S. cerevisiae CET1 when coexpressed with pombe ceg1

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GO biological process

GO:0006370 - 7-methylguanosine mRNA capping

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GO cellular component

GO:0005634 - nucleus

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GO:0031533 - mRNA capping enzyme complex

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GO molecular function

GO:0016887 - ATP hydrolysis activity

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GO:0140818 - mRNA 5'-triphosphate monophosphatase activity

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GO:0004651 - polynucleotide 5'-phosphatase activity

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GO:0005515 - protein binding

References:

GO:0099122 - RNA polymerase II C-terminal domain binding

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Modification

MOD:01149 - sumoylated lysine

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MOD:01148 - ubiquitinylated lysine

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Quantitative gene expression

PBO:0006310 - protein level

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PBO:0011963 - RNA level

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Single locus phenotype

FYPO:0003674 - abolished ATPase activity

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Genotypes:

FYPO:0004299 - abolished polynucleotide 5'-phosphatase activity

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Genotypes:

FYPO:0000705 - abolished protein-protein interaction

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Genotypes:

FYPO:0001168 - decreased ATPase activity

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Genotypes:

FYPO:0000311 - inviable after spore germination with normal, unseptated germ tube morphology

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Genotypes:

FYPO:0002430 - inviable after spore germination, multiple cell divisions

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Genotypes:

FYPO:0002151 - inviable spore

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Genotypes:

FYPO:0002061 - inviable vegetative cell population

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Genotypes:

FYPO:0001387 - loss of viability at high temperature

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Genotypes:

FYPO:0004300 - normal ATPase activity

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Genotypes:

FYPO:0000703 - normal protein-protein interaction

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Genotypes:

FYPO:0002060 - viable vegetative cell population

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Genotypes:

Subunit composition

PBO:0015212 - homomeric(2)

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Taxonomic conservation

PBO:0011065 - conserved in eukaryotes

PBO:0011064 - conserved in fungi

PBO:0011069 - conserved in metazoa

PBO:0011070 - conserved in vertebrates

PBO:0006222 - predominantly single copy (one to one)

Protein features

IDNameInterPro nameDB name
PF02940mRNA_triPasemRNA_triPase_Cet1PFAM
cd07470CYTH-like_mRNA_RTPasemRNA_triPase_Cet1CDD
SSF55154CYTH-like phosphatasesCYTH-like_dom_sfSUPERFAMILY
G3DSA:3.20.100.10mRNA_triPase_Cet1_sfGENE3D
PTHR28118POLYNUCLEOTIDE 5'-TRIPHOSPHATASE-RELATEDCet1/Ctl1PANTHER

Orthologs

References / Literature

PMID:23101633 - Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells.
Marguerat S et al. Cell 2012 Oct 26;151(3):671-83
PMID:23697806 - A genome-wide resource of cell cycle and cell shape genes of fission yeast.
Hayles J et al. Open Biol 2013 May 22;3(5):130053
PMID:20473289 - Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe.
Kim DU et al. Nat Biotechnol 2010 Jun;28(6):617-623
PMID:24763107 - Absolute proteome and phosphoproteome dynamics during the cell cycle of Schizosaccharomyces pombe (Fission Yeast).
Carpy A et al. Mol Cell Proteomics 2014 Aug;13(8):1925-36
PMID:11387325 - The length, phosphorylation state, and primary structure of the RNA polymerase II carboxyl-terminal domain dictate interactions with mRNA capping enzymes.
Pei Y et al. J Biol Chem 2001 Jul 27;276(30):28075-82
PMID:21511999 - Comparative functional genomics of the fission yeasts.
Rhind N et al. Science 2011 May 20;332(6032):930-6
PMID:26537787 - Targeting of SUMO substrates to a Cdc48-Ufd1-Npl4 segregase and STUbL pathway in fission yeast.
Køhler JB et al. Nat Commun 2015 Nov 05;6:8827
PMID:37970674 - SUMOylation regulates Lem2 function in centromere clustering and silencing.
Strachan J et al. J Cell Sci 2023 Dec 01;136(23)
PMID:12475973 - Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality control.
Pei Y et al. J Biol Chem 2003 Feb 28;278(9):7180-8
PMID:25414009 - Fission yeast RNA triphosphatase reads an Spt5 CTD code.
Doamekpor SK et al. RNA 2015 Jan;21(1):113-23
PMID:11737862 - RNA triphosphatase is essential in Schizosaccharomyces pombe and Candida albicans.
Pei Y et al. BMC Microbiol 2001;1:29
PMID:11139608 - Characterization of Schizosaccharomyces pombe RNA triphosphatase.
Pei Y et al. Nucleic Acids Res 2001 Jan 15;29(2):387-96
PMID:11751918 - The fission yeast ES2 homologue, Bis1, interacts with the Ish1 stress-responsive nuclear envelope protein.
Taricani L et al. J Biol Chem 2002 Mar 22;277(12):10562-72
PMID:12788946 - Homodimeric quaternary structure is required for the in vivo function and thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe RNA triphosphatases.
Hausmann S et al. J Biol Chem 2003 Aug 15;278(33):30487-96
PMID:16428435 - Cyclin-dependent kinase 9 (Cdk9) of fission yeast is activated by the CDK-activating kinase Csk1, overlaps functionally with the TFIIH-associated kinase Mcs6, and associates with the mRNA cap methyltransferase Pcm1 in vivo.
Pei Y et al. Mol Cell Biol 2006 Feb;26(3):777-88
PMID:16823372 - ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.
Matsuyama A et al. Nat Biotechnol 2006 Jul;24(7):841-7
PMID:16980382 - Genetic evidence for phospholipid-mediated regulation of the Rab GDP-dissociation inhibitor in fission yeast.
Ma Y et al. Genetics 2006 Nov;174(3):1259-71
PMID:12637515 - Physical and functional interaction of the yeast corepressor Tup1 with mRNA 5'-triphosphatase.
Mukai Y et al. J Biol Chem 2003 May 23;278(21):18895-901
GO_REF:0000002 - Comments
PMID:20231361 - Separable functions of the fission yeast Spt5 carboxyl-terminal domain (CTD) in capping enzyme binding and transcription elongation overlap with those of the RNA polymerase II CTD.
Schneider S et al. Mol Cell Biol 2010 May;30(10):2353-64
PMID:12455993 - Divergent subunit interactions among fungal mRNA 5'-capping machineries.
Takagi T et al. Eukaryot Cell 2002 Jun;1(3):448-57
PMID:11893740 - Interactions between fission yeast mRNA capping enzymes and elongation factor Spt5.
Pei Y et al. J Biol Chem 2002 May 31;277(22):19639-48
PMID:22508988 - Separate domains of fission yeast Cdk9 (P-TEFb) are required for capping enzyme recruitment and primed (Ser7-phosphorylated) Rpb1 carboxyl-terminal domain substrate recognition.
St Amour CV et al. Mol Cell Biol 2012 Jul;32(13):2372-83