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Protein

mRNA-capping enzyme subunit beta

Gene

pct1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.1 Publication

Catalytic activityi

A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate.

Cofactori

a divalent metal cationBy similarityNote: Divalent metal ions.By similarity

GO - Molecular functioni

  • ATPase activity Source: PomBase
  • polynucleotide 5'-phosphatase activity Source: PomBase

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: PomBase
  • 7-methylguanosine RNA capping Source: PomBase
  • polynucleotide 5' dephosphorylation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA capping, mRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-capping enzyme subunit beta (EC:3.1.3.33)
Alternative name(s):
Polynucleotide 5'-triphosphatase
mRNA 5'-triphosphatase
Short name:
TPase
Gene namesi
Name:pct1
ORF Names:SPAC644.04
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC644.04.
PomBaseiSPAC644.04. pct1.

Subcellular locationi

GO - Cellular componenti

  • mRNA cap methyltransferase complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303mRNA-capping enzyme subunit betaPRO_0000210117Add
BLAST

Proteomic databases

MaxQBiQ9P6Q6.

Interactioni

Subunit structurei

The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
cdk9Q96WV92EBI-443547,EBI-443557

Protein-protein interaction databases

BioGridi280085. 7 interactions.
IntActiQ9P6Q6. 2 interactions.
MINTiMINT-4704598.

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 6712Combined sources
Turni68 – 714Combined sources
Beta strandi77 – 8812Combined sources
Turni89 – 924Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi103 – 1053Combined sources
Helixi107 – 1115Combined sources
Beta strandi112 – 1165Combined sources
Helixi121 – 13717Combined sources
Beta strandi147 – 15913Combined sources
Beta strandi167 – 17610Combined sources
Beta strandi179 – 19416Combined sources
Beta strandi201 – 21111Combined sources
Beta strandi222 – 23413Combined sources
Beta strandi237 – 2459Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi256 – 2649Combined sources
Helixi266 – 27712Combined sources
Helixi282 – 29918Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PN0X-ray2.60A/B/C/D1-303[»]
4PN1X-ray2.80A/B/C/D1-303[»]
ProteinModelPortaliQ9P6Q6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the fungal TPase family.Curated

Phylogenomic databases

InParanoidiQ9P6Q6.
OMAiTHYLITE.
OrthoDBiEOG7FZ07W.
PhylomeDBiQ9P6Q6.

Family and domain databases

Gene3Di3.20.100.10. 1 hit.
InterProiIPR033469. CYTH-like_dom.
IPR004206. mRNA_triPase_Cet1.
[Graphical view]
PfamiPF02940. mRNA_triPase. 1 hit.
[Graphical view]
SUPFAMiSSF55154. SSF55154. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9P6Q6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLKGLLHEE NELPSIEKRK IDENAVEHDK VERKRTKSVA VPKIEMNFLN
60 70 80 90 100
KPIVPDTTKV ISNFLTHYLI TEPVEHVEIE AKLGTLIDLE TQNRFEFPVM
110 120 130 140 150
NETILNPEFN LRTRFESDMT ASEHKYLNEF LNQAFRDSQK PGRLPFAYKH
160 170 180 190 200
TKQVDLFYET EDNSRDKIRV SKNQSDNQVL ACVKKRRVAD LFLYCPNDAF
210 220 230 240 250
DIRISISDEL PVSMPSGNQQ PSLTRLKDRV GYVHQEIKID LTKTTQNDPV
260 270 280 290 300
YDTTERHELE VEFGNIADLR DRAQKAKDGM EAPLFRRVQL FMDNVRILRR

EHS
Length:303
Mass (Da):35,444
Last modified:October 1, 2000 - v1
Checksum:i51A5A112CE927AED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB90131.1.
RefSeqiNP_593872.1. NM_001019302.2.

Genome annotation databases

EnsemblFungiiSPAC644.04.1; SPAC644.04.1:pep; SPAC644.04.
GeneIDi2543671.
KEGGispo:SPAC644.04.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB90131.1.
RefSeqiNP_593872.1. NM_001019302.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PN0X-ray2.60A/B/C/D1-303[»]
4PN1X-ray2.80A/B/C/D1-303[»]
ProteinModelPortaliQ9P6Q6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280085. 7 interactions.
IntActiQ9P6Q6. 2 interactions.
MINTiMINT-4704598.

Proteomic databases

MaxQBiQ9P6Q6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC644.04.1; SPAC644.04.1:pep; SPAC644.04.
GeneIDi2543671.
KEGGispo:SPAC644.04.

Organism-specific databases

EuPathDBiFungiDB:SPAC644.04.
PomBaseiSPAC644.04. pct1.

Phylogenomic databases

InParanoidiQ9P6Q6.
OMAiTHYLITE.
OrthoDBiEOG7FZ07W.
PhylomeDBiQ9P6Q6.

Miscellaneous databases

NextBioi20804677.
PROiQ9P6Q6.

Family and domain databases

Gene3Di3.20.100.10. 1 hit.
InterProiIPR033469. CYTH-like_dom.
IPR004206. mRNA_triPase_Cet1.
[Graphical view]
PfamiPF02940. mRNA_triPase. 1 hit.
[Graphical view]
SUPFAMiSSF55154. SSF55154. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Homodimeric quaternary structure is required for the in vivo function and thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe RNA triphosphatases."
    Hausmann S., Pei Y., Shuman S.
    J. Biol. Chem. 278:30487-30496(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.

Entry informationi

Entry nameiCET1_SCHPO
AccessioniPrimary (citable) accession number: Q9P6Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.