SPS2_PIG
ID SPS2_PIG Reviewed; 451 AA.
AC A1YIZ1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 70.
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 AltName: Full=Selenophosphate synthase 2;
GN Name=SEPHS2; Synonyms=SPS2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RA Zhou J.C., Zhao H., Wang K.N., Li J.G., Rocha P., Xia X.J., Lei X.G.;
RT "The expression of SPS2 in Sus scrofa affected by dietary selenium.";
RL Submitted (JAN-2007) 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 subunit. {ECO:0000250|UniProtKB:P49903};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49903}.
CC -!- PTM: Truncated SEPHS2 proteins produced by failed UGA/Sec decoding are
CC ubiquitinated by the CRL2(KLHDC3) complex, which recognizes the glycine
CC (Gly) at the C-terminus of truncated SEPHS2 proteins.
CC {ECO:0000250|UniProtKB:Q99611}.
CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I
CC subfamily. {ECO:0000305}.
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DR EMBL; EF033624; ABM46855.1; -; mRNA.
DR RefSeq; NP_001087204.1; NM_001093735.1.
DR PeptideAtlas; A1YIZ1; -.
DR Ensembl; ENSSSCT00030095354; ENSSSCP00030043937; ENSSSCG00030068190.
DR Ensembl; ENSSSCT00035086280; ENSSSCP00035035935; ENSSSCG00035064131.
DR Ensembl; ENSSSCT00040044154; ENSSSCP00040018556; ENSSSCG00040032793.
DR Ensembl; ENSSSCT00055054932; ENSSSCP00055043833; ENSSSCG00055027768.
DR Ensembl; ENSSSCT00060105907; ENSSSCP00060046661; ENSSSCG00060077040.
DR GeneID; 100037302; -.
DR KEGG; ssc:100037302; -.
DR CTD; 22928; -.
DR InParanoid; A1YIZ1; -.
DR OrthoDB; 1166567at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00476; selD; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Selenium;
KW Selenocysteine; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99611"
FT CHAIN 2..451
FT /note="Selenide, water dikinase 2"
FT /id="PRO_0000312763"
FT ACT_SITE 63
FT /evidence="ECO:0000255"
FT BINDING 66
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 121..123
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 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 141
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 164
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 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 215..218
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 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT SITE 66
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P16456"
FT NON_STD 63
FT /note="Selenocysteine"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99611"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97364"
SQ SEQUENCE 451 AA; 47821 MW; 50CC5DAD4226F195 CRC64;
MAEAAATGAG GEMMAAVAAG EGCSGPAGLS LGRGFSGYRP FEPQALGLSP SWRLTGFSGM
KGUGCKVPQE TLLKLLAGLT RPEVRPPVGR GLVGGLEEAA QEAGLPVRAE PSPTFPTLGI
GLDSCVIPLR HGGLSLVQTT DFFYPLVEDP YMMGRIACAN VLSDLYAMGI TECDNMLMLL
SVSQNMIEEE REKITPLMIK GFRDAAEEGG TAVTGGQTVI NPWIIIGGVA TVVCQPNEFI
MPDSAVVGDV LVLTKPLGTQ VAVNAHQWLD NPERWNKIKM VVSREEVELA YQEAMFNMAT
LNRTAAGLMH TFNAHAATDI TGFGILGHSQ NLAKQQRNEV SFVIHNLPII AKMAAISKAS
GRFGLLQGTS AETSGGLLIC LPREQAARFC SEIKSSKYGE GHQAWIVGIV EKGNRTARII
DKPRVIEVLP RGTAATALAP ENSSASSEPS L
