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Q9P6Q5 (DUT_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable deoxyuridine 5'-triphosphate nucleotidohydrolase

Short name=dUTPase
EC=3.6.1.23
Alternative name(s):
dUTP pyrophosphatase
Gene names
ORF Names:SPAC644.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length140 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA By similarity.

Catalytic activity

dUTP + H2O = dUMP + diphosphate.

Cofactor

Magnesium By similarity.

Pathway

Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.

Subunit structure

Homotrimer By similarity.

Sequence similarities

Belongs to the dUTPase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 140140Probable deoxyuridine 5'-triphosphate nucleotidohydrolase
PRO_0000182935

Regions

Region62 – 643Substrate binding By similarity
Region76 – 794Substrate binding By similarity
Region135 – 1362Substrate binding By similarity

Sites

Binding site1301Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9P6Q5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3C8F2FCC9AAE2CCE

FASTA14014,862
        10         20         30         40         50         60 
MSFFVQKLSE KATIPTKGSA NSAGYDLYAA AECIVPRRGK VLVDTDLAIA VPEGTYGRVA 

        70         80         90        100        110        120 
PRSGLASKHS IDTGAGVIDA DYRGHVRVLL FNYSDVDFPI KVGDRIAQLI LERIVNPPVI 

       130        140 
LVESLEATVR GANGFGSTGV 

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB90132.1.
RefSeqNP_593873.1. NM_001019303.2.

3D structure databases

ProteinModelPortalQ9P6Q5.
SMRQ9P6Q5. Positions 3-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4704587.
STRING4896.SPAC644.05c-1.

Proteomic databases

PaxDbQ9P6Q5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC644.05c.1; SPAC644.05c.1:pep; SPAC644.05c.
GeneID2543669.
KEGGspo:SPAC644.05c.

Organism-specific databases

PomBaseSPAC644.05c.

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028966.
KOK01520.
OMALVDTQIS.
OrthoDBEOG7T7H6C.
PhylomeDBQ9P6Q5.

Enzyme and pathway databases

UniPathwayUPA00610; UER00666.

Family and domain databases

InterProIPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00576. dut. 1 hit.
ProtoNetSearch...

Other

NextBio20804675.
PROQ9P6Q5.

Entry information

Entry nameDUT_SCHPO
AccessionPrimary (citable) accession number: Q9P6Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways