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Protein
Submitted name:

DUTPase

Gene

dut

Organism
Leishmania major
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi48 – 481Calcium 1Combined sources
Metal bindingi48 – 481Calcium 2Combined sources
Metal bindingi48 – 481MagnesiumCombined sources
Metal bindingi51 – 511Calcium 1Combined sources
Metal bindingi51 – 511Calcium 2Combined sources
Metal bindingi51 – 511MagnesiumCombined sources
Metal bindingi76 – 761Calcium 2Combined sources
Metal bindingi76 – 761MagnesiumCombined sources
Metal bindingi79 – 791Calcium 2Combined sources
Metal bindingi79 – 791MagnesiumCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseImported

Keywords - Ligandi

CalciumCombined sources, MagnesiumCombined sources, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
DUTPaseImported (EC:3.6.1.23Imported)
Submitted name:
Putative deoxyuridine triphosphataseImported
Gene namesi
Name:dutImported
Synonyms:DUTImported
ORF Names:LMJF_06_0560Imported
OrganismiLeishmania majorImported
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
Proteomesi
  • UP000000542 Componenti: Chromosome 6

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4418.

Interactioni

Protein-protein interaction databases

STRINGi5664.LmjF.06.0560.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CJEX-ray2.34A1-268[»]
2YAYX-ray1.86A1-268[»]
2YAZX-ray2.40A/B/D/E1-268[»]
2YB0X-ray2.28A/B/D/E1-268[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410K2HU. Eukaryota.
ENOG4112CGJ. LUCA.
HOGENOMiHOG000255273.
KOiK01520.
OMAiFRQDHGY.

Family and domain databases

InterProiIPR014871. dUTPase/dCTP_pyrophosphatase.
[Graphical view]
PfamiPF08761. dUTPase_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15826-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRARSANIP GAILHSLAEL QDGLNAMIDP SWRAVRSLDN WALAITMEST
60 70 80 90 100
ELLDSYPWKW WKNLNATPDL ANVRIELVDI FHFSLSGAMQ MRSTPDDEIP
110 120 130 140 150
AASLKPLKEV MTTFLPAKEC TSDPYGFVFF PLTDTQNAIA SFRNIIQLAN
160 170 180 190 200
AYRFDVIIEC IIYAAEDLGF NLVAYYIAKH TLNCIRQLSG YKDGSYVKVN
210 220 230 240 250
NGVEDNSLLH NCIKDVSLDE VLDADKYVQA WNSIMANVYE AFQIKESDRK
260
DAERWFALAK ENRLAIKA
Length:268
Mass (Da):30,354
Last modified:January 1, 1998 - v1
Checksum:iB1F230CD5752F5F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76742 mRNA. Translation: AAC02795.1.
FR796402 Genomic DNA. Translation: CAJ02101.1.
RefSeqiXP_001680826.1. XM_001680774.1.

Genome annotation databases

EnsemblProtistsiLmjF.06.0560:mRNA; LmjF.06.0560:pep; LmjF.06.0560.
GeneIDi5649078.
KEGGilma:LMJF_06_0560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76742 mRNA. Translation: AAC02795.1.
FR796402 Genomic DNA. Translation: CAJ02101.1.
RefSeqiXP_001680826.1. XM_001680774.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CJEX-ray2.34A1-268[»]
2YAYX-ray1.86A1-268[»]
2YAZX-ray2.40A/B/D/E1-268[»]
2YB0X-ray2.28A/B/D/E1-268[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5664.LmjF.06.0560.

Chemistry

ChEMBLiCHEMBL4418.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiLmjF.06.0560:mRNA; LmjF.06.0560:pep; LmjF.06.0560.
GeneIDi5649078.
KEGGilma:LMJF_06_0560.

Phylogenomic databases

eggNOGiENOG410K2HU. Eukaryota.
ENOG4112CGJ. LUCA.
HOGENOMiHOG000255273.
KOiK01520.
OMAiFRQDHGY.

Family and domain databases

InterProiIPR014871. dUTPase/dCTP_pyrophosphatase.
[Graphical view]
PfamiPF08761. dUTPase_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Description of a novel eukaryotic deoxyuridine 5'-triphosphate nucleotidohydrolase in Leishmania major."
    Camacho A., Arrebola R., Pena-Diaz J., Ruiz-Perez L.M., Gonzalez-Pacanowska D.
    Biochem. J. 325:441-447(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 252Imported.
  2. "The genome of the kinetoplastid parasite, Leishmania major."
    Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., Bianchettin G.
    , Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S., Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B., Myler P.J.
    Science 309:436-442(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FriedlinImported and MHOM/IL/81/FriedlinImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FriedlinImported and MHOM/IL/81/FriedlinImported.
  4. "The crystal structure of the Leishmania major deoxyuridine triphosphate nucleotidohydrolase in complex with nucleotide analogues, dUMP, and deoxyuridine."
    Hemsworth G.R., Moroz O.V., Fogg M.J., Scott B., Bosch-Navarrete C., Gonzalez-Pacanowska D., Wilson K.S.
    J. Biol. Chem. 286:16470-16481(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH CALCIUM AND MAGNESIUM.
  5. Zhao B.P., Ren Z.A., Li C.D.
    Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: FriedlinImported.

Entry informationi

Entry nameiO15826_LEIMA
AccessioniPrimary (citable) accession number: O15826
Secondary accession number(s): Q4QJ22
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.