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Reviewed, UniProtKB/Swiss-Prot Q9VKY8 (SPS2_DROME)

Last modified February 9, 2010. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Selenide, water dikinase 2
    EC=2.7.9.3
Alternative name(s):
    Selenophosphate synthetase 2
    Selenium donor protein 2
      Short name=Dsps2
Gene names
Name: Sps2
ORF Names: CG5025
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Synthesizes selenophosphate from selenide and ATP.

Catalytic activity

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

Tissue specificity

First expressed in the midgut anlagen with subsequent expression in a variety of tissues including the gut and nervous system. Ref.1

Developmental stage

Expressed both maternally and zygotically. Ref.1

Sequence similarities

Belongs to the selenophosphate synthetase 1 family. Class I subfamily.

Sequence caution

The sequence AAR99143.1 differs from that shown. Reason: Erroneous termination at position 24. Translated as Sec.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Selenocysteine
   LigandATP-binding
Nucleotide-binding
Selenium
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processselenocysteine biosynthetic process Ref.1

Traceable author statement. Source: UniProtKB

   Molecular functionATP binding Ref.1

Traceable author statement. Source: UniProtKB

selenide, water dikinase activity Ref.1

Traceable author statement. Source: UniProtKB

selenium binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9VKY8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q9VKY8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     279-305: VLFQINKLPIIKNVLKFSTLVGQSTKF → HLGGPKHKVSIWQIGGNLWRPFNMPSC
     306-370: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflict2791H → P in AAF80118. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Selenide, water dikinase 2
PRO_0000127653

Regions

Nucleotide binding261 – 2677ATP Potential

Sites

Active site241 Potential
Site271Important for catalytic activity By similarity

Amino acid modifications

Non-standard residue241Selenocysteine

Natural variations

Alternative sequence279 – 30527VLFQI…QSTKF → HLGGPKHKVSIWQIGGNLWR PFNMPSC in isoform B.
VSP_050768
Alternative sequence306 – 37065Missing in isoform B.
VSP_050769

Experimental info

Sequence conflict1891L → F Ref.2
Sequence conflict1891L → F Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: 95128BCD133731B3

FASTA37041,131
        10         20         30         40         50         60 
MFQPEKHGLE PDFQLTKFTT HTGUSCKIPQ KVLEKYLRGT EIENKNNDGY LIGSGMDCAV 

        70         80         90        100        110        120 
IPLKRHKDYL LIQTVDFFYP MVNDPELLGR IALANVLSDV YAVGVTQFDT VEMIVSTSTS 

       130        140        150        160        170        180 
FSEKERDVVI GLVMKGFQNS LKANGYRNTP LIIRQLKINP WCIIGGIATS VCRSEEIILP 

       190        200        210        220        230        240 
SNAQPGDVLV LTKPLGGQMA MDAHLWQLNQ TEKYKKLLSE CSDADIKETF EIAVKSMTYL 

       250        260        270        280        290        300 
NKNAALLMHK YQAHCATDIT GFGLLGHANN LAQFQKEKVL FQINKLPIIK NVLKFSTLVG 

       310        320        330        340        350        360 
QSTKFRSGRS VETSGGLLIC LPADAADKFC RDFEEATNGE QKSFQIGHVT AANESDAVLC 

       370 
EDVEFIEVSL 

« Hide

Isoform B.

Checksum: 59C8805F98948F5A
Show »

FASTA30534,155

References

« Hide 'large scale' references
[1]"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: 11258485] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM A), PROBABLE SELENOCYSTEINE AT SEC-24, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Embryo.
[2]"Structural analysis of new local features in SECIS RNA hairpins."
Fagegaltier D., Lescure A., Walczak R., Carbon P., Krol A.
Nucleic Acids Res. 28:2679-2689(2000) [PubMed: 10908323] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
[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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[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: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ278068 mRNA. Translation: CAB93526.2.
AF279253 mRNA. Translation: AAF80118.1.
AE014134 Genomic DNA. Translation: AAF52918.2.
AE014134 Genomic DNA. Translation: AAN10746.2.
BT011485 mRNA. Translation: AAR99143.1. Sequence problems.
RefSeqNP_477477.4.
NP_477478.4.
UniGeneDm.3457

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9VKY8. 4 interactions.
STRINGQ9VKY8.

Genome annotation databases

EnsemblFBtr0079997; FBpp0079587; FBgn0032224; Drosophila melanogaster. [Genome view]
FBtr0079998; FBpp0079588; FBgn0032224; Drosophila melanogaster. [Genome view]
GeneID34397.
KEGGdme:Dmel_CG5025.

Organism-specific databases

CTD34397.
FlyBaseFBgn0032224. Sps2.

Phylogenomic databases

InParanoidQ9VKY8.
OMAGISANIW.
PhylomeDBQ9VKY8.

Enzyme and pathway databases

BRENDA2.7.9.3. 48.

Gene expression databases

BgeeQ9VKY8.
GermOnlineCG5025. Drosophila melanogaster.

Family and domain databases

InterProIPR000728. AIR_synth.
IPR010918. AIR_synth_C.
IPR016188. PurM_N-like.
IPR004536. SelD.
[Graphical view]
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
PIRSFPIRSF036407. Selenphspht_syn. 1 hit.
TIGRFAMsTIGR00476. selD. 1 hit.
ProtoNetSearch...

Other Resources

NextBio788302.

Entry information

Entry nameSPS2_DROME
AccessionPrimary (citable) accession number: Q9VKY8
Secondary accession number(s): Q8IPC0, Q9NAX3, Q9NFK7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: February 26, 2008
Last modified: February 9, 2010
This is version 59 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents