Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Deoxynucleoside kinase

Gene

dnk

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Deoxyribonucleoside kinase that has a broad specificity phosphorylating thymidine, 2'-deoxyriboadenosine, 2'-deoxydeoxycytidine and 2'-deoxydeoxyguanosine. Specificity is higher for pyrimidine nucleosides. Several anti-viral and anti-cancer nucleoside analogs are also efficiently phosphorylated.3 Publications

Catalytic activityi

ATP + a 2'-deoxyribonucleoside = ADP + a 2'-deoxyribonucleoside 5'-phosphate.4 Publications

Enzyme regulationi

Subject to feedback inhibition by dTTP.1 Publication

Kineticsi

  1. KM=0.9 µM for thymidine2 Publications
  2. KM=1 µM for deoxycytidine2 Publications
  3. KM=109 µM for deoxyadenosine2 Publications
  4. KM=654 µM for deoxyguanosine2 Publications
  1. Vmax=29.4 mmol/min/mg enzyme with thymidine as substrate2 Publications
  2. Vmax=28.7 mmol/min/mg enzyme with deoxycytidine as substrate2 Publications
  3. Vmax=35.5 mmol/min/mg enzyme with deoxyadenosine as substrate2 Publications
  4. Vmax=37.7 mmol/min/mg enzyme with deoxyguanosine as substrate2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei52Substrate1
Binding sitei70Substrate1
Binding sitei81Substrate1
Active sitei104Proton acceptorSequence analysis1
Binding sitei105Substrate1
Binding sitei172Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi27 – 35ATPBy similarity9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • deoxynucleoside kinase activity Source: UniProtKB
  • kinase activity Source: FlyBase

GO - Biological processi

  • DNA biosynthetic process Source: UniProtKB-KW
  • nucleoside diphosphate phosphorylation Source: UniProtKB
  • nucleotide phosphorylation Source: FlyBase
  • phosphorylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

DNA synthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17889.
BRENDAi2.7.1.145. 1994.
ReactomeiR-DME-73614. Pyrimidine salvage reactions.
R-DME-74217. Purine salvage.
SABIO-RKQ9XZT6.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxynucleoside kinase (EC:2.7.1.1454 Publications)
Alternative name(s):
Deoxyribonucleoside kinase
Short name:
Dm-dNK
Multispecific deoxynucleoside kinase
Gene namesi
Name:dnk
ORF Names:CG5452
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0022338. dnk.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi45N → D: Reduces enzyme activity towards dA, dG, dT and dC about 5-fold. 1 Publication1
Mutagenesisi64N → D: Reduces enzyme activity towards dT and dC about 500-fold. Reduces enzyme activity towards dG about 3900-fold. Reduces enzyme activity towards dA about 900-fold. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4760.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001750971 – 250Deoxynucleoside kinaseAdd BLAST250

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei236Phosphoserine1 Publication1
Modified residuei241Phosphoserine1 Publication1
Modified residuei243Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9XZT6.
PRIDEiQ9XZT6.

PTM databases

iPTMnetiQ9XZT6.

Expressioni

Gene expression databases

BgeeiFBgn0022338.
ExpressionAtlasiQ9XZT6. baseline.
GenevisibleiQ9XZT6. DM.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi67276. 8 interactors.
DIPiDIP-23491N.
IntActiQ9XZT6. 1 interactor.
MINTiMINT-879155.
STRINGi7227.FBpp0302815.

Chemistry databases

BindingDBiQ9XZT6.

Structurei

Secondary structure

1250
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni15 – 17Combined sources3
Beta strandi21 – 28Combined sources8
Helixi33 – 38Combined sources6
Helixi39 – 43Combined sources5
Turni44 – 46Combined sources3
Beta strandi47 – 50Combined sources4
Helixi54 – 57Combined sources4
Beta strandi60 – 62Combined sources3
Helixi65 – 71Combined sources7
Helixi73 – 93Combined sources21
Beta strandi98 – 105Combined sources8
Helixi107 – 112Combined sources6
Helixi114 – 120Combined sources7
Beta strandi122 – 124Combined sources3
Helixi126 – 142Combined sources17
Beta strandi148 – 154Combined sources7
Helixi157 – 167Combined sources11
Helixi170 – 172Combined sources3
Helixi177 – 191Combined sources15
Turni192 – 194Combined sources3
Beta strandi200 – 206Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J90X-ray2.56A/B1-230[»]
1OE0X-ray2.40A/B/C/D1-230[»]
1OT3X-ray2.50A/B/C/D/E/F/G/H1-250[»]
1ZM7X-ray2.20A/B/C/D1-230[»]
1ZMXX-ray3.10A/B/C/D/E/F/G/H1-230[»]
2JCSX-ray2.50A/B1-230[»]
2JJ8X-ray2.80A/B/C/D1-230[»]
2VP0X-ray2.20A/B1-250[»]
2VP2X-ray2.50A/B1-230[»]
2VP4X-ray2.20A/B/C/D1-230[»]
2VP5X-ray2.30A/B1-230[»]
2VP6X-ray3.00A/B/C/D/E/F/G/H1-230[»]
2VP9X-ray2.90A/B/C/D/E/F/G/H1-230[»]
2VPPX-ray2.20A/B1-230[»]
2VQSX-ray2.90A/B/C/D1-230[»]
ProteinModelPortaliQ9XZT6.
SMRiQ9XZT6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9XZT6.

Family & Domainsi

Sequence similaritiesi

Belongs to the DCK/DGK family.Curated

Phylogenomic databases

eggNOGiKOG4235. Eukaryota.
COG1428. LUCA.
GeneTreeiENSGT00510000046588.
InParanoidiQ9XZT6.
KOiK05961.
OMAiMYRDACR.
OrthoDBiEOG091G0PXX.
PhylomeDBiQ9XZT6.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR002624. DCK/DGK.
IPR031314. DNK_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01712. dNK. 1 hit.
[Graphical view]
PIRSFiPIRSF000705. DNK. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9XZT6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEAASCARK GTKYAEGTQP FTVLIEGNIG SGKTTYLNHF EKYKNDICLL
60 70 80 90 100
TEPVEKWRNV NGVNLLELMY KDPKKWAMPF QSYVTLTMLQ SHTAPTNKKL
110 120 130 140 150
KIMERSIFSA RYCFVENMRR NGSLEQGMYN TLEEWYKFIE ESIHVQADLI
160 170 180 190 200
IYLRTSPEVA YERIRQRARS EESCVPLKYL QELHELHEDW LIHQRRPQSC
210 220 230 240 250
KVLVLDADLN LENIGTEYQR SESSIFDAIS SNQQPSPVLV SPSKRQRVAR
Length:250
Mass (Da):29,088
Last modified:November 1, 1999 - v1
Checksum:i17C5DF197B8792DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF045610 mRNA. Translation: AAD47355.2.
AF185268 Genomic DNA. Translation: AAD56545.1.
Y18048 mRNA. Translation: CAB41881.1.
AE014297 Genomic DNA. Translation: AAF55615.1.
RefSeqiNP_001262722.1. NM_001275793.1.
NP_524399.1. NM_079675.3.
UniGeneiDm.1248.

Genome annotation databases

EnsemblMetazoaiFBtr0083707; FBpp0083121; FBgn0022338.
FBtr0321263; FBpp0302815; FBgn0022338.
GeneIDi42273.
KEGGidme:Dmel_CG5452.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF045610 mRNA. Translation: AAD47355.2.
AF185268 Genomic DNA. Translation: AAD56545.1.
Y18048 mRNA. Translation: CAB41881.1.
AE014297 Genomic DNA. Translation: AAF55615.1.
RefSeqiNP_001262722.1. NM_001275793.1.
NP_524399.1. NM_079675.3.
UniGeneiDm.1248.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J90X-ray2.56A/B1-230[»]
1OE0X-ray2.40A/B/C/D1-230[»]
1OT3X-ray2.50A/B/C/D/E/F/G/H1-250[»]
1ZM7X-ray2.20A/B/C/D1-230[»]
1ZMXX-ray3.10A/B/C/D/E/F/G/H1-230[»]
2JCSX-ray2.50A/B1-230[»]
2JJ8X-ray2.80A/B/C/D1-230[»]
2VP0X-ray2.20A/B1-250[»]
2VP2X-ray2.50A/B1-230[»]
2VP4X-ray2.20A/B/C/D1-230[»]
2VP5X-ray2.30A/B1-230[»]
2VP6X-ray3.00A/B/C/D/E/F/G/H1-230[»]
2VP9X-ray2.90A/B/C/D/E/F/G/H1-230[»]
2VPPX-ray2.20A/B1-230[»]
2VQSX-ray2.90A/B/C/D1-230[»]
ProteinModelPortaliQ9XZT6.
SMRiQ9XZT6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67276. 8 interactors.
DIPiDIP-23491N.
IntActiQ9XZT6. 1 interactor.
MINTiMINT-879155.
STRINGi7227.FBpp0302815.

Chemistry databases

BindingDBiQ9XZT6.
ChEMBLiCHEMBL4760.

PTM databases

iPTMnetiQ9XZT6.

Proteomic databases

PaxDbiQ9XZT6.
PRIDEiQ9XZT6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0083707; FBpp0083121; FBgn0022338.
FBtr0321263; FBpp0302815; FBgn0022338.
GeneIDi42273.
KEGGidme:Dmel_CG5452.

Organism-specific databases

CTDi42273.
FlyBaseiFBgn0022338. dnk.

Phylogenomic databases

eggNOGiKOG4235. Eukaryota.
COG1428. LUCA.
GeneTreeiENSGT00510000046588.
InParanoidiQ9XZT6.
KOiK05961.
OMAiMYRDACR.
OrthoDBiEOG091G0PXX.
PhylomeDBiQ9XZT6.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17889.
BRENDAi2.7.1.145. 1994.
ReactomeiR-DME-73614. Pyrimidine salvage reactions.
R-DME-74217. Purine salvage.
SABIO-RKQ9XZT6.

Miscellaneous databases

EvolutionaryTraceiQ9XZT6.
GenomeRNAii42273.
PROiQ9XZT6.

Gene expression databases

BgeeiFBgn0022338.
ExpressionAtlasiQ9XZT6. baseline.
GenevisibleiQ9XZT6. DM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR002624. DCK/DGK.
IPR031314. DNK_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01712. dNK. 1 hit.
[Graphical view]
PIRSFiPIRSF000705. DNK. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDNK_DROME
AccessioniPrimary (citable) accession number: Q9XZT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.