SPS2_DROME
ID SPS2_DROME Reviewed; 370 AA.
AC Q9VKY8; Q8IPC0; Q9NAX3; Q9NFK7;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Selenide, water dikinase 2;
DE EC=2.7.9.3 {ECO:0000250|UniProtKB:P49903};
DE AltName: Full=Selenium donor protein 2;
DE Short=Dsps2;
DE AltName: Full=Selenophosphate synthase 2;
GN Name=Sps2; ORFNames=CG5025;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM A), PROBABLE SELENOCYSTEINE AT SEC-24, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=11258485; DOI=10.1093/embo-reports/kvd087;
RA Hirosawa-Takamori M., Jackle H., Vorbruggen G.;
RT "The class 2 selenophosphate synthetase gene of Drosophila contains a
RT functional mammalian-type SECIS.";
RL EMBO Rep. 1:441-446(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RX PubMed=10908323; DOI=10.1093/nar/28.14.2679;
RA Fagegaltier D., Lescure A., Walczak R., Carbon P., Krol A.;
RT "Structural analysis of new local features in SECIS RNA hairpins.";
RL Nucleic Acids Res. 28:2679-2689(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
CC {ECO:0000250|UniProtKB:P49903}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate +
CC selenophosphate; Xref=Rhea:RHEA:18737, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16144, ChEBI:CHEBI:29317,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; EC=2.7.9.3;
CC Evidence={ECO:0000250|UniProtKB:P49903};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P49903};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P49903};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49903}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9VKY8-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9VKY8-2; Sequence=VSP_050768, VSP_050769;
CC -!- TISSUE SPECIFICITY: First expressed in the midgut anlagen with
CC subsequent expression in a variety of tissues including the gut and
CC nervous system. {ECO:0000269|PubMed:11258485}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:11258485}.
CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR99143.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ278068; CAB93526.2; -; mRNA.
DR EMBL; AF279253; AAF80118.1; -; mRNA.
DR EMBL; AE014134; AAF52918.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10746.2; -; Genomic_DNA.
DR EMBL; BT011485; AAR99143.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001260329.1; NM_001273400.2. [Q9VKY8-1]
DR RefSeq; NP_477478.4; NM_058130.6. [Q9VKY8-1]
DR BioGRID; 60482; 4.
DR IntAct; Q9VKY8; 1.
DR STRING; 7227.FBpp0079588; -.
DR PaxDb; Q9VKY8; -.
DR PRIDE; Q9VKY8; -.
DR EnsemblMetazoa; FBtr0079998; FBpp0079588; FBgn0032224. [Q9VKY8-1]
DR EnsemblMetazoa; FBtr0310115; FBpp0301800; FBgn0032224. [Q9VKY8-1]
DR GeneID; 34397; -.
DR KEGG; dme:Dmel_CG5025; -.
DR CTD; 34397; -.
DR FlyBase; FBgn0032224; Sps2.
DR VEuPathDB; VectorBase:FBgn0032224; -.
DR eggNOG; KOG3939; Eukaryota.
DR GeneTree; ENSGT00390000000950; -.
DR HOGENOM; CLU_032859_1_0_1; -.
DR InParanoid; Q9VKY8; -.
DR OMA; INPWCIV; -.
DR PhylomeDB; Q9VKY8; -.
DR BRENDA; 2.7.9.3; 1994.
DR BioGRID-ORCS; 34397; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34397; -.
DR PRO; PR:Q9VKY8; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032224; Expressed in crop (Drosophila) and 28 other tissues.
DR ExpressionAtlas; Q9VKY8; baseline and differential.
DR Genevisible; Q9VKY8; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017076; F:purine nucleotide binding; ISS:FlyBase.
DR GO; GO:0004756; F:selenide, water dikinase activity; ISS:FlyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016260; P:selenocysteine biosynthetic process; ISS:FlyBase.
DR CDD; cd02195; SelD; 1.
DR Gene3D; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 1.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR004536; SPS/SelD.
DR PANTHER; PTHR10256; PTHR10256; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR PIRSF; PIRSF036407; Selenphspht_syn; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00476; selD; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Selenium; Selenocysteine;
KW Transferase.
FT CHAIN 1..370
FT /note="Selenide, water dikinase 2"
FT /id="PRO_0000127653"
FT ACT_SITE 24
FT /evidence="ECO:0000255"
FT BINDING 27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 55..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT SITE 27
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P16456"
FT NON_STD 24
FT /note="Selenocysteine"
FT VAR_SEQ 279..305
FT /note="VLFQINKLPIIKNVLKFSTLVGQSTKF -> HLGGPKHKVSIWQIGGNLWRP
FT FNMPSC (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10908323,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_050768"
FT VAR_SEQ 306..370
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10908323,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_050769"
FT CONFLICT 189
FT /note="L -> F (in Ref. 2 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9VKY8-2:279
FT /note="H -> P (in Ref. 2; AAF80118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 41131 MW; 95128BCD133731B3 CRC64;
MFQPEKHGLE PDFQLTKFTT HTGUSCKIPQ KVLEKYLRGT EIENKNNDGY LIGSGMDCAV
IPLKRHKDYL LIQTVDFFYP MVNDPELLGR IALANVLSDV YAVGVTQFDT VEMIVSTSTS
FSEKERDVVI GLVMKGFQNS LKANGYRNTP LIIRQLKINP WCIIGGIATS VCRSEEIILP
SNAQPGDVLV LTKPLGGQMA MDAHLWQLNQ TEKYKKLLSE CSDADIKETF EIAVKSMTYL
NKNAALLMHK YQAHCATDIT GFGLLGHANN LAQFQKEKVL FQINKLPIIK NVLKFSTLVG
QSTKFRSGRS VETSGGLLIC LPADAADKFC RDFEEATNGE QKSFQIGHVT AANESDAVLC
EDVEFIEVSL
