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Protein

Selenide, water dikinase

Gene

SelD

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

Functioni

Synthesizes selenophosphate from selenide and ATP. Essential for progression of the cell cycle by controlling the synthesis of selenoproteins. Plays a role in apoptosis and consequently a role in imaginal disk patterning and growth.4 Publications

Catalytic activityi

ATP + selenide + H2O = AMP + selenophosphate + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei51 – 511Sequence analysis
Sitei52 – 521Important for catalytic activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi290 – 2967ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell proliferation Source: FlyBase
  • glutamine metabolic process Source: FlyBase
  • imaginal disc development Source: FlyBase
  • mitochondrion organization Source: FlyBase
  • negative regulation of reactive oxygen species metabolic process Source: FlyBase
  • neurogenesis Source: FlyBase
  • positive regulation of cell proliferation Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • selenocysteine biosynthetic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding, Selenium

Names & Taxonomyi

Protein namesi
Recommended name:
Selenide, water dikinase (EC:2.7.9.3)
Alternative name(s):
Protein patufet
Selenium donor protein
Selenophosphate synthase
dSelD
Gene namesi
Name:SelD
Synonyms:PTF1, ptuf
ORF Names:CG8553
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0261270. SelD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Selenide, water dikinasePRO_0000127652Add
BLAST

Proteomic databases

PaxDbiO18373.
PRIDEiO18373.

Expressioni

Tissue specificityi

Expressed at low levels throughout the embryo. At later developmental stages, expressed in areas of high cell proliferation. From embryo stage 13, expression is high in central nervous system and midgut, especially in the gastric caeca. Expression also seen in larval imaginal disks and brain.3 Publications

Developmental stagei

Throughout development, from embryo to adult.1 Publication

Gene expression databases

BgeeiO18373.
GenevisibleiO18373. DM.

Interactioni

Protein-protein interaction databases

BioGridi62337. 12 interactions.
DIPiDIP-21887N.
IntActiO18373. 6 interactions.
MINTiMINT-898227.
STRINGi7227.FBpp0086691.

Structurei

3D structure databases

ProteinModelPortaliO18373.
SMRiO18373. Positions 27-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3939. Eukaryota.
COG0709. LUCA.
GeneTreeiENSGT00390000000950.
InParanoidiO18373.
KOiK01008.
OMAiMMAIAIL.
OrthoDBiEOG7SR4MT.
PhylomeDBiO18373.

Family and domain databases

Gene3Di3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR016188. PurM-like_N.
IPR004536. SPS/SelD.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
PIRSFiPIRSF036407. Selenphspht_syn. 1 hit.
SUPFAMiSSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR00476. selD. 1 hit.

Sequencei

Sequence statusi: Complete.

O18373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYAADVLNS AHLELHGGGD AELRRPFDPT AHDLDASFRL TRFADLKGRG
60 70 80 90 100
CKVPQDVLSK LVSALQQDYS AQDQEPQFLN VAIPRIGIGL DCSVIPLRHG
110 120 130 140 150
GLCLVQTTDF FYPIVDDPYM MGKIACANVL SDLYAMGVTD CDNMLMLLAV
160 170 180 190 200
STKMTEKERD VVIPLIMRGF KDSALEAGTT VTGGQSVVNP WCTIGGVAST
210 220 230 240 250
ICQPNEYIVP DNAVVGDVLV LTKPLGTQVA VNAHQWIDQP ERWNRIKLVV
260 270 280 290 300
SEEDVRKAYH RAMNSMARLN RVAARLMHKY NAHGATDITG FGLLGHAQTL
310 320 330 340 350
AAHQKKDVSF VIHNLPVIAK MAAVAKACGN MFQLLQGHSA ETSGGLLICL
360 370 380 390
PREQAAAYCK DIEKQEGYQA WIIGIVEKGN KTARIIDKPR VIEVPAKD
Length:398
Mass (Da):43,446
Last modified:January 1, 1998 - v1
Checksum:iB265DAF4FDACC2D8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2542ED → KN in AAB88790 (PubMed:9491069).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ000672 mRNA. Translation: CAA04229.1.
U91994 Genomic DNA. Translation: AAB88790.1.
AE013599 Genomic DNA. Translation: AAF58266.1.
AY095058 mRNA. Translation: AAM11386.1.
RefSeqiNP_725374.1. NM_166045.2.
NP_725375.1. NM_166046.2.
UniGeneiDm.2979.

Genome annotation databases

EnsemblMetazoaiFBtr0087564; FBpp0086690; FBgn0261270.
FBtr0087565; FBpp0086691; FBgn0261270.
GeneIDi36587.
KEGGidme:Dmel_CG8553.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ000672 mRNA. Translation: CAA04229.1.
U91994 Genomic DNA. Translation: AAB88790.1.
AE013599 Genomic DNA. Translation: AAF58266.1.
AY095058 mRNA. Translation: AAM11386.1.
RefSeqiNP_725374.1. NM_166045.2.
NP_725375.1. NM_166046.2.
UniGeneiDm.2979.

3D structure databases

ProteinModelPortaliO18373.
SMRiO18373. Positions 27-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62337. 12 interactions.
DIPiDIP-21887N.
IntActiO18373. 6 interactions.
MINTiMINT-898227.
STRINGi7227.FBpp0086691.

Proteomic databases

PaxDbiO18373.
PRIDEiO18373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087564; FBpp0086690; FBgn0261270.
FBtr0087565; FBpp0086691; FBgn0261270.
GeneIDi36587.
KEGGidme:Dmel_CG8553.

Organism-specific databases

CTDi36587.
FlyBaseiFBgn0261270. SelD.

Phylogenomic databases

eggNOGiKOG3939. Eukaryota.
COG0709. LUCA.
GeneTreeiENSGT00390000000950.
InParanoidiO18373.
KOiK01008.
OMAiMMAIAIL.
OrthoDBiEOG7SR4MT.
PhylomeDBiO18373.

Miscellaneous databases

GenomeRNAii36587.
PROiO18373.

Gene expression databases

BgeeiO18373.
GenevisibleiO18373. DM.

Family and domain databases

Gene3Di3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR016188. PurM-like_N.
IPR004536. SPS/SelD.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
PIRSFiPIRSF036407. Selenphspht_syn. 1 hit.
SUPFAMiSSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR00476. selD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SelD homolog from Drosophila lacking selenide-dependent monoselenophosphate synthetase activity."
    Persson B.C., Boeck A., Jaeckle H., Vorbrueggen G.
    J. Mol. Biol. 274:174-180(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: Canton-S.
    Tissue: Embryo.
  2. "patufet, the gene encoding the Drosophila melanogaster homologue of selenophosphate synthetase, is involved in imaginal disc morphogenesis."
    Alsina B., Serras F., Baguna J., Corominas M.
    Mol. Gen. Genet. 257:113-123(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Disruption of selenoprotein biosynthesis affects cell proliferation in the imaginal discs and brain of Drosophila melanogaster."
    Alsina B., Corominas M., Berry M.J., Baguna J., Serras F.
    J. Cell Sci. 112:2875-2884(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  7. "The class 2 selenophosphate synthetase gene of Drosophila contains a functional mammalian-type SECIS."
    Hirosawa-Takamori M., Jackle H., Vorbruggen G.
    EMBO Rep. 1:441-446(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiSPS1_DROME
AccessioniPrimary (citable) accession number: O18373
Secondary accession number(s): O18597, Q0E979, Q9V700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: June 8, 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

Caution

The conserved active site Cys (or selenocysteine) residue in position 49 is replaced by an Arg. However, as function in selenoprotein synthesis is proven, it is possible Cys-51 is the active site.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.