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Q6E4Q0

- DUT_ANTLO

UniProt

Q6E4Q0 - DUT_ANTLO

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Protein
Deoxyuridine 5'-triphosphate nucleotidohydrolase
Gene
DUT1
Organism
Antonospora locustae (Microsporidian parasite) (Nosema locustae)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

dUTP + H2O = dUMP + diphosphate.

Cofactori

Magnesium By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei132 – 1321Substrate By similarity

GO - Molecular functioni

  1. dUTP diphosphatase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. dUMP biosynthetic process Source: UniProtKB-UniPathway
  2. dUTP metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00610; UER00666.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase (EC:3.6.1.23)
Short name:
dUTPase
Alternative name(s):
dUTP pyrophosphatase
Gene namesi
Name:DUT1
OrganismiAntonospora locustae (Microsporidian parasite) (Nosema locustae)
Taxonomic identifieri278021 [NCBI]
Taxonomic lineageiEukaryotaFungiMicrosporidiaAntonospora

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 143143Deoxyuridine 5'-triphosphate nucleotidohydrolase
PRO_0000182927Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ6E4Q0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 663Substrate binding By similarity
Regioni78 – 814Substrate binding By similarity
Regioni137 – 1382Substrate binding By similarity

Sequence similaritiesi

Belongs to the dUTPase family.

Family and domain databases

Gene3Di2.70.40.10. 1 hit.
InterProiIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR008181. dUTPase_1.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.
TIGRFAMsiTIGR00576. dut. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6E4Q0-1 [UniParc]FASTAAdd to Basket

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MSEIITVKRL FSDAKIPVRH SEGAAAYDLY AYEDTVVAPN ERKVIATGVR    50
ITVPLSCQGT IYSRSGLALK YCIEIFGVNI GPGETKDIVV DIYNHGKMPF 100
NVAKGDRIAQ IVFIKLFGGD LHEVSELSDT KRGSCGWGST GIS 143
Length:143
Mass (Da):15,526
Last modified:August 16, 2004 - v1
Checksum:iF8E434A8A47CBA8C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY574349 Genomic DNA. Translation: AAT72741.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY574349 Genomic DNA. Translation: AAT72741.1 .

3D structure databases

ProteinModelPortali Q6E4Q0.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00610 ; UER00666 .

Family and domain databases

Gene3Di 2.70.40.10. 1 hit.
InterProi IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR008181. dUTPase_1.
[Graphical view ]
Pfami PF00692. dUTPase. 1 hit.
[Graphical view ]
SUPFAMi SSF51283. SSF51283. 1 hit.
TIGRFAMsi TIGR00576. dut. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genome compaction and stability in microsporidian intracellular parasites."
    Slamovits C.H., Fast N.M., Law J.S., Keeling P.J.
    Curr. Biol. 14:891-896(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiDUT_ANTLO
AccessioniPrimary (citable) accession number: Q6E4Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: August 16, 2004
Last modified: June 11, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3