ID   SPS1_BOVIN              Reviewed;         392 AA.
AC   Q0VC82;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Selenide, water dikinase 1;
DE            EC=2.7.9.3 {ECO:0000250|UniProtKB:P49903};
DE   AltName: Full=Selenium donor protein 1;
DE   AltName: Full=Selenophosphate synthase 1;
GN   Name=SEPHS1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 monomer. {ECO:0000250|UniProtKB:P49903};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49903}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P49903};
CC       Peripheral membrane protein {ECO:0000305}. Nucleus membrane
CC       {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein
CC       {ECO:0000305}.
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 probable, it is possible Cys-31 is the active site.
CC       {ECO:0000305}.
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DR   EMBL; BC120303; AAI20304.1; -; mRNA.
DR   RefSeq; NP_001068784.1; NM_001075316.1.
DR   RefSeq; XP_005214232.1; XM_005214175.3.
DR   AlphaFoldDB; Q0VC82; -.
DR   SMR; Q0VC82; -.
DR   STRING; 9913.ENSBTAP00000011613; -.
DR   PaxDb; Q0VC82; -.
DR   PRIDE; Q0VC82; -.
DR   Ensembl; ENSBTAT00000011613; ENSBTAP00000011613; ENSBTAG00000008821.
DR   Ensembl; ENSBTAT00000075258; ENSBTAP00000061100; ENSBTAG00000008821.
DR   GeneID; 507470; -.
DR   KEGG; bta:507470; -.
DR   CTD; 22929; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008821; -.
DR   VGNC; VGNC:34448; SEPHS1.
DR   eggNOG; KOG3939; Eukaryota.
DR   GeneTree; ENSGT00390000000950; -.
DR   HOGENOM; CLU_032859_1_0_1; -.
DR   InParanoid; Q0VC82; -.
DR   OMA; DNEPKYG; -.
DR   OrthoDB; 1166567at2759; -.
DR   TreeFam; TF313811; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000008821; Expressed in thymus and 110 other tissues.
DR   ExpressionAtlas; Q0VC82; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS: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: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   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cell membrane; Kinase; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Selenium;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P49903"
FT   CHAIN           2..392
FT                   /note="Selenide, water dikinase 1"
FT                   /id="PRO_0000312506"
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:0000250|UniProtKB:P49903"
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:0000250|UniProtKB:P49903"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P49903"
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:0000250|UniProtKB:P49903"
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:0000250|UniProtKB:P49903"
FT   BINDING         110
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P49903"
FT   BINDING         161..164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P49903"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P49903"
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:0000250|UniProtKB:P49903"
SQ   SEQUENCE   392 AA;  42881 MW;  A9D73E72449BB394 CRC64;
     MSARESFNPE 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