ID   SPS1_HUMAN              Reviewed;         392 AA.
AC   P49903; B4DWK0; D3DRS9; D6PSQ9; Q5T5U8; Q5T5U9; Q9BVT4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2002, sequence version 2.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Selenide, water dikinase 1;
DE            EC=2.7.9.3 {ECO:0000269|PubMed:7665581};
DE   AltName: Full=Selenium donor protein 1;
DE   AltName: Full=Selenophosphate synthase 1;
GN   Name=SEPHS1; Synonyms=SELD, SPS, SPS1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   ATP-BINDING, AND MUTAGENESIS OF GLY-268; GLY-270; GLY-273 AND HIS-274.
RC   TISSUE=Liver;
RX   PubMed=7665581; DOI=10.1074/jbc.270.37.21659;
RA   Low S.C., Harney J.W., Berry M.J.;
RT   "Cloning and functional characterization of human selenophosphate
RT   synthetase, an essential component of selenoprotein synthesis.";
RL   J. Biol. Chem. 270:21659-21664(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBUNIT, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20471958; DOI=10.1016/j.bbrc.2010.05.055;
RA   Kim J.Y., Lee K.H., Shim M.S., Shin H., Xu X.M., Carlson B.A.,
RA   Hatfield D.L., Lee B.J.;
RT   "Human selenophosphate synthetase 1 has five splice variants with unique
RT   interactions, subcellular localizations and expression patterns.";
RL   Biochem. Biophys. Res. Commun. 397:53-58(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Mammary gland;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta, and PNS;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 5-16 AND 64-76, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Fetal brain cortex;
RA   Lubec G., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADP; MAGNESIUM IONS
RP   AND PHOSPHATE, SUBUNIT, ACTIVITY REGULATION, AND MUTAGENESIS OF THR-85.
RX   PubMed=19477186; DOI=10.1016/j.jmb.2009.05.032;
RA   Wang K.T., Wang J., Li L.F., Su X.D.;
RT   "Crystal structures of catalytic intermediates of human selenophosphate
RT   synthetase 1.";
RL   J. Mol. Biol. 390:747-759(2009).
CC   -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
CC       {ECO:0000269|PubMed:7665581}.
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:0000269|PubMed:7665581};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:19477186};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000269|PubMed:19477186};
CC   -!- ACTIVITY REGULATION: Activated by phosphate ions and by potassium ions.
CC       {ECO:0000269|PubMed:19477186}.
CC   -!- SUBUNIT: [Isoform 1]: Homodimer (PubMed:20471958, PubMed:19477186).
CC       Heterodimer with isoform 3 (PubMed:20471958).
CC       {ECO:0000269|PubMed:19477186, ECO:0000269|PubMed:20471958}.
CC   -!- SUBUNIT: [Isoform 2]: Homodimer (PubMed:20471958). Heterodimer with
CC       isoform 4 (PubMed:20471958). {ECO:0000269|PubMed:20471958}.
CC   -!- SUBUNIT: [Isoform 3]: Homodimer (PubMed:20471958). Heterodimer with
CC       isoform 1 (PubMed:20471958). {ECO:0000269|PubMed:20471958}.
CC   -!- SUBUNIT: [Isoform 4]: Homodimer (PubMed:20471958). Heterodimer with
CC       isoform 2 (PubMed:20471958). {ECO:0000269|PubMed:20471958}.
CC   -!- INTERACTION:
CC       P49903; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-714091, EBI-2876622;
CC       P49903; Q2TAL8: QRICH1; NbExp=8; IntAct=EBI-714091, EBI-2798044;
CC       P49903; P49903: SEPHS1; NbExp=6; IntAct=EBI-714091, EBI-714091;
CC       P49903; Q6GPH4: XAF1; NbExp=3; IntAct=EBI-714091, EBI-2815120;
CC       P49903; P24278: ZBTB25; NbExp=7; IntAct=EBI-714091, EBI-739899;
CC       P49903; O95125: ZNF202; NbExp=5; IntAct=EBI-714091, EBI-751960;
CC       P49903; Q8N554: ZNF276; NbExp=3; IntAct=EBI-714091, EBI-750821;
CC       P49903; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-714091, EBI-17269964;
CC       P49903; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-714091, EBI-11035148;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC       {ECO:0000269|PubMed:20471958}; Peripheral membrane protein
CC       {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:20471958};
CC       Peripheral membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000269|PubMed:20471958}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC       {ECO:0000269|PubMed:20471958}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm
CC       {ECO:0000269|PubMed:20471958}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Major type, MT;
CC         IsoId=P49903-1; Sequence=Displayed;
CC       Name=2; Synonyms=Delta E8;
CC         IsoId=P49903-2; Sequence=VSP_046702;
CC       Name=3; Synonyms=Delta E2;
CC         IsoId=P49903-3; Sequence=VSP_046701;
CC       Name=4; Synonyms=E9, E9a;
CC         IsoId=P49903-4; Sequence=VSP_047451;
CC   -!- TISSUE SPECIFICITY: [Isoform 1]: Gradually expressed during the cell
CC       cycle until G2/M phase and then decreases.
CC       {ECO:0000269|PubMed:20471958}.
CC   -!- TISSUE SPECIFICITY: [Isoform 2]: Gradually expressed during the cell
CC       cycle until G2/M phase and then decreases.
CC       {ECO:0000269|PubMed:20471958}.
CC   -!- TISSUE SPECIFICITY: [Isoform 3]: Gradually expressed during the cell
CC       cycle until S phase and then decreases. {ECO:0000269|PubMed:20471958}.
CC   -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class II
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: The conserved active site Cys (or selenocysteine) residue in
CC       position 29 is replaced by a Thr. However, as function in selenoprotein
CC       synthesis is proven, it is possible Cys-31 is the active site.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA87567.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U34044; AAA87567.1; ALT_FRAME; mRNA.
DR   EMBL; GU954545; ADF78120.1; -; mRNA.
DR   EMBL; GU954546; ADF78121.1; -; mRNA.
DR   EMBL; GU954547; ADF78122.1; -; mRNA.
DR   EMBL; GU954548; ADF78123.1; -; mRNA.
DR   EMBL; GU954549; ADF78124.1; -; mRNA.
DR   EMBL; AK301568; BAG63062.1; -; mRNA.
DR   EMBL; AL138764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL355870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471072; EAW86289.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW86290.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW86291.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW86292.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW86293.1; -; Genomic_DNA.
DR   EMBL; BC000941; AAH00941.1; -; mRNA.
DR   EMBL; BC063816; AAH63816.1; -; mRNA.
DR   CCDS; CCDS55702.1; -. [P49903-3]
DR   CCDS; CCDS55703.1; -. [P49903-2]
DR   CCDS; CCDS7098.1; -. [P49903-1]
DR   RefSeq; NP_001182531.1; NM_001195602.1. [P49903-3]
DR   RefSeq; NP_001182533.1; NM_001195604.1. [P49903-2]
DR   RefSeq; NP_036379.2; NM_012247.4. [P49903-1]
DR   RefSeq; XP_016871431.1; XM_017015942.1.
DR   RefSeq; XP_016871432.1; XM_017015943.1.
DR   RefSeq; XP_016871434.1; XM_017015945.1.
DR   PDB; 3FD5; X-ray; 1.90 A; A/B=1-392.
DR   PDB; 3FD6; X-ray; 1.95 A; A/B=1-392.
DR   PDBsum; 3FD5; -.
DR   PDBsum; 3FD6; -.
DR   AlphaFoldDB; P49903; -.
DR   SMR; P49903; -.
DR   BioGRID; 116589; 73.
DR   CORUM; P49903; -.
DR   IntAct; P49903; 25.
DR   MINT; P49903; -.
DR   STRING; 9606.ENSP00000367893; -.
DR   GlyGen; P49903; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P49903; -.
DR   MetOSite; P49903; -.
DR   PhosphoSitePlus; P49903; -.
DR   SwissPalm; P49903; -.
DR   BioMuta; SEPHS1; -.
DR   DMDM; 27151792; -.
DR   EPD; P49903; -.
DR   jPOST; P49903; -.
DR   MassIVE; P49903; -.
DR   MaxQB; P49903; -.
DR   PaxDb; 9606-ENSP00000367893; -.
DR   PeptideAtlas; P49903; -.
DR   ProteomicsDB; 12836; -.
DR   ProteomicsDB; 5348; -.
DR   ProteomicsDB; 56175; -. [P49903-1]
DR   ProteomicsDB; 64555; -.
DR   Pumba; P49903; -.
DR   Antibodypedia; 24810; 225 antibodies from 30 providers.
DR   DNASU; 22929; -.
DR   Ensembl; ENST00000327347.10; ENSP00000367893.3; ENSG00000086475.15. [P49903-1]
DR   Ensembl; ENST00000378614.8; ENSP00000367877.3; ENSG00000086475.15. [P49903-2]
DR   Ensembl; ENST00000545675.5; ENSP00000441119.2; ENSG00000086475.15. [P49903-3]
DR   GeneID; 22929; -.
DR   KEGG; hsa:22929; -.
DR   MANE-Select; ENST00000327347.10; ENSP00000367893.3; NM_012247.5; NP_036379.2.
DR   UCSC; uc001imk.4; human. [P49903-1]
DR   AGR; HGNC:19685; -.
DR   CTD; 22929; -.
DR   DisGeNET; 22929; -.
DR   GeneCards; SEPHS1; -.
DR   HGNC; HGNC:19685; SEPHS1.
DR   HPA; ENSG00000086475; Low tissue specificity.
DR   MIM; 600902; gene.
DR   neXtProt; NX_P49903; -.
DR   OpenTargets; ENSG00000086475; -.
DR   PharmGKB; PA134905215; -.
DR   VEuPathDB; HostDB:ENSG00000086475; -.
DR   eggNOG; KOG3939; Eukaryota.
DR   GeneTree; ENSGT00390000000950; -.
DR   HOGENOM; CLU_032859_1_0_1; -.
DR   InParanoid; P49903; -.
DR   OMA; LARDWMC; -.
DR   OrthoDB; 177624at2759; -.
DR   PhylomeDB; P49903; -.
DR   TreeFam; TF313811; -.
DR   BRENDA; 2.7.9.3; 2681.
DR   PathwayCommons; P49903; -.
DR   SignaLink; P49903; -.
DR   BioGRID-ORCS; 22929; 143 hits in 1159 CRISPR screens.
DR   ChiTaRS; SEPHS1; human.
DR   EvolutionaryTrace; P49903; -.
DR   GeneWiki; Selenophosphate_synthetase_1; -.
DR   GenomeRNAi; 22929; -.
DR   Pharos; P49903; Tbio.
DR   PRO; PR:P49903; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; P49903; Protein.
DR   Bgee; ENSG00000086475; Expressed in ventricular zone and 202 other cell types or tissues.
DR   ExpressionAtlas; P49903; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR   GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0004756; F:selenide, water dikinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IBA:GO_Central.
DR   CDD; cd02195; SelD; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR016188; PurM-like_N.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR004536; SPS/SelD.
DR   NCBIfam; TIGR00476; selD; 1.
DR   PANTHER; PTHR10256; SELENIDE, WATER DIKINASE; 1.
DR   PANTHER; PTHR10256:SF2; SELENIDE, WATER DIKINASE 1; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   PIRSF; PIRSF036407; Selenphspht_syn; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
DR   Genevisible; P49903; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Cell membrane; Cytoplasm; Direct protein sequencing; Kinase; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Selenium; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..392
FT                   /note="Selenide, water dikinase 1"
FT                   /id="PRO_0000127648"
FT   ACT_SITE        31
FT                   /evidence="ECO:0000255"
FT   BINDING         32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:19477186,
FT                   ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6"
FT   BINDING         67..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:19477186,
FT                   ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:19477186,
FT                   ECO:0007744|PDB:3FD6"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:19477186,
FT                   ECO:0007744|PDB:3FD5"
FT   BINDING         110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:19477186,
FT                   ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6"
FT   BINDING         110
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:19477186,
FT                   ECO:0007744|PDB:3FD6"
FT   BINDING         161..164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000269|PubMed:19477186,
FT                   ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:19477186,
FT                   ECO:0007744|PDB:3FD6"
FT   SITE            32
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P16456"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   VAR_SEQ         1..67
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:20471958"
FT                   /id="VSP_046701"
FT   VAR_SEQ         251..321
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:20471958"
FT                   /id="VSP_046702"
FT   VAR_SEQ         322..392
FT                   /note="GGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRII
FT                   EVAPQVATQNVNPTPGATS -> DVQ (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:20471958"
FT                   /id="VSP_047451"
FT   MUTAGEN         85
FT                   /note="T->A: Strongly reduced ADP hydrolysis."
FT                   /evidence="ECO:0000269|PubMed:19477186"
FT   MUTAGEN         268
FT                   /note="G->C: No change in ATP-binding."
FT                   /evidence="ECO:0000269|PubMed:7665581"
FT   MUTAGEN         270
FT                   /note="G->R: No change in ATP-binding."
FT                   /evidence="ECO:0000269|PubMed:7665581"
FT   MUTAGEN         273
FT                   /note="G->A,D,V: Loss of ATP-binding."
FT                   /evidence="ECO:0000269|PubMed:7665581"
FT   MUTAGEN         274
FT                   /note="H->N: Reduced ATP-binding."
FT                   /evidence="ECO:0000269|PubMed:7665581"
FT   MUTAGEN         274
FT                   /note="H->Y: Increased ATP-binding."
FT                   /evidence="ECO:0000269|PubMed:7665581"
FT   CONFLICT        260
FT                   /note="A -> T (in Ref. 1; AAA87567)"
FT                   /evidence="ECO:0000305"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           20..23
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           35..42
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   STRAND          68..74
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   STRAND          81..89
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           96..113
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   STRAND          120..129
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           134..154
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   STRAND          159..169
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   STRAND          171..180
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           182..184
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   STRAND          196..201
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           205..213
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           218..224
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           230..245
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           249..257
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   STRAND          262..265
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           270..279
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   STRAND          283..296
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           299..305
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   TURN            306..308
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           312..314
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   STRAND          324..328
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   HELIX           330..341
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   STRAND          352..362
FT                   /evidence="ECO:0007829|PDB:3FD5"
FT   STRAND          364..375
FT                   /evidence="ECO:0007829|PDB:3FD5"
SQ   SEQUENCE   392 AA;  42911 MW;  E9636E38146D926D CRC64;
     MSTRESFNPE SYELDKSFRL TRFTELKGTG CKVPQDVLQK LLESLQENHF QEDEQFLGAV
     MPRLGIGMDT CVIPLRHGGL SLVQTTDYIY PIVDDPYMMG RIACANVLSD LYAMGVTECD
     NMLMLLGVSN KMTDRERDKV MPLIIQGFKD AAEEAGTSVT GGQTVLNPWI VLGGVATTVC
     QPNEFIMPDN AVPGDVLVLT KPLGTQVAVA VHQWLDIPEK WNKIKLVVTQ EDVELAYQEA
     MMNMARLNRT AAGLMHTFNA HAATDITGFG ILGHAQNLAK QQRNEVSFVI HNLPVLAKMA
     AVSKACGNMF GLMHGTCPET SGGLLICLPR EQAARFCAEI KSPKYGEGHQ AWIIGIVEKG
     NRTARIIDKP RIIEVAPQVA TQNVNPTPGA TS
//