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 07-APR-2021, entry version 181. 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}; 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; 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. [P49903-1] 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 SMR; P49903; -. DR BioGRID; 116589; 59. DR CORUM; P49903; -. DR IntAct; P49903; 22. DR MINT; P49903; -. DR STRING; 9606.ENSP00000367893; -. 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; P49903; -. DR PeptideAtlas; P49903; -. DR PRIDE; P49903; -. DR ProteomicsDB; 12836; -. DR ProteomicsDB; 5348; -. DR ProteomicsDB; 56175; -. [P49903-1] DR ProteomicsDB; 64555; -. DR Antibodypedia; 24810; 188 antibodies. DR DNASU; 22929; -. DR Ensembl; ENST00000327347; ENSP00000367893; ENSG00000086475. [P49903-1] DR Ensembl; ENST00000378614; ENSP00000367877; ENSG00000086475. [P49903-2] DR Ensembl; ENST00000545675; ENSP00000441119; ENSG00000086475. [P49903-3] DR GeneID; 22929; -. DR KEGG; hsa:22929; -. DR UCSC; uc001imk.4; human. [P49903-1] 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:ENSG00000086475.14; -. DR eggNOG; KOG3939; Eukaryota. DR GeneTree; ENSGT00390000000950; -. DR HOGENOM; CLU_032859_1_0_1; -. DR InParanoid; P49903; -. DR OMA; MNIVCFP; -. DR OrthoDB; 1166567at2759; -. DR PhylomeDB; P49903; -. DR TreeFam; TF313811; -. DR BRENDA; 2.7.9.3; 2681. DR PathwayCommons; P49903; -. DR BioGRID-ORCS; 22929; 126 hits in 996 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 female gonad and 231 other tissues. DR ExpressionAtlas; P49903; baseline and differential. DR Genevisible; P49903; HS. 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:0006464; P:cellular protein modification process; TAS:ProtInc. DR GO; GO:0016260; P:selenocysteine biosynthetic process; IBA:GO_Central. 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; IPR016188; PurM-like_N. DR InterPro; IPR036921; PurM-like_N_sf. DR InterPro; IPR004536; SPS/SelD. DR PANTHER; PTHR10256; PTHR10256; 1. DR Pfam; PF00586; AIRS; 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 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 NP_BIND 67..69 FT /note="ATP" FT /evidence="ECO:0000269|PubMed:19477186, FT ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6" FT NP_BIND 161..164 FT /note="ATP; shared with dimeric partner" FT /evidence="ECO:0000269|PubMed:19477186, FT ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6" FT ACT_SITE 31 FT /evidence="ECO:0000255" FT METAL 69 FT /note="Magnesium" FT /evidence="ECO:0000269|PubMed:19477186, FT ECO:0007744|PDB:3FD6" FT METAL 110 FT /note="Magnesium" FT /evidence="ECO:0000269|PubMed:19477186, FT ECO:0007744|PDB:3FD6" FT METAL 265 FT /note="Magnesium" FT /evidence="ECO:0000269|PubMed:19477186, FT ECO:0007744|PDB:3FD6" FT BINDING 32 FT /note="ATP" FT /evidence="ECO:0000269|PubMed:19477186, FT ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6" FT BINDING 87 FT /note="ATP" FT /evidence="ECO:0000269|PubMed:19477186, FT ECO:0007744|PDB:3FD5" FT BINDING 110 FT /note="ATP" FT /evidence="ECO:0000269|PubMed:19477186, FT ECO:0007744|PDB:3FD5, 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:0007744|PDB:3FD5" FT HELIX 20..23 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 35..42 FT /evidence="ECO:0007744|PDB:3FD5" FT STRAND 68..74 FT /evidence="ECO:0007744|PDB:3FD5" FT STRAND 81..89 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 96..113 FT /evidence="ECO:0007744|PDB:3FD5" FT STRAND 120..129 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 134..154 FT /evidence="ECO:0007744|PDB:3FD5" FT STRAND 159..169 FT /evidence="ECO:0007744|PDB:3FD5" FT STRAND 171..180 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 182..184 FT /evidence="ECO:0007744|PDB:3FD5" FT STRAND 196..201 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 205..213 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 218..224 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 230..245 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 249..257 FT /evidence="ECO:0007744|PDB:3FD5" FT STRAND 262..265 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 270..279 FT /evidence="ECO:0007744|PDB:3FD5" FT STRAND 283..296 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 299..305 FT /evidence="ECO:0007744|PDB:3FD5" FT TURN 306..308 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 312..314 FT /evidence="ECO:0007744|PDB:3FD5" FT STRAND 324..328 FT /evidence="ECO:0007744|PDB:3FD5" FT HELIX 330..341 FT /evidence="ECO:0007744|PDB:3FD5" FT STRAND 352..362 FT /evidence="ECO:0007744|PDB:3FD5" FT STRAND 364..375 FT /evidence="ECO:0007744|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 //