ID V8P6U9_OPHHA Unreviewed; 362 AA.
AC V8P6U9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Selenide, water dikinase 1 {ECO:0000256|ARBA:ARBA00039825};
DE EC=2.7.9.3 {ECO:0000256|ARBA:ARBA00011997};
DE AltName: Full=Selenium donor protein 1 {ECO:0000256|ARBA:ARBA00042811};
DE AltName: Full=Selenophosphate synthase 1 {ECO:0000256|ARBA:ARBA00042724};
DE Flags: Fragment;
GN Name=SEPHS1 {ECO:0000313|EMBL:ETE69743.1};
GN ORFNames=L345_04443 {ECO:0000313|EMBL:ETE69743.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE69743.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE69743.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE69743.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
CC {ECO:0000256|ARBA:ARBA00003786}.
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:0000256|ARBA:ARBA00001359};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Nucleus membrane
CC {ECO:0000256|ARBA:ARBA00004617}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004617}.
CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class II
CC subfamily. {ECO:0000256|ARBA:ARBA00038427}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE69743.1}.
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DR EMBL; AZIM01000703; ETE69743.1; -; Genomic_DNA.
DR AlphaFoldDB; V8P6U9; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004756; F:selenide, water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ETE69743.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Selenium {ECO:0000256|ARBA:ARBA00023266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 50..155
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 174..336
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE69743.1"
SQ SEQUENCE 362 AA; 39584 MW; 5EBB2822AA20E3C0 CRC64;
MSTGRRKSAV TNRVRIMSVR ESFNPESYEL DKSFRLTRFT ELKGTGIGMD TCVIPLRHGG
LSLVQTTDYI YPIVDDPYMM GRIACANVLS DLYAMGVTEC DNMLMLLGIS NKMTDRERDK
IMPLIIQGFK DAAEEAGTSV TGGQTVLNPW IVLGGVATTV CQPNEFIMPD NAVPGDVLVL
TKPLGTQVAV AVHQWLDIPE KWNKIKLVVT QEDVELAYQE AMMNMARLNR TAAGLMHTFN
AHAATDITGF GILGHAQNLA KQQRNEVSFV IHNLPVLAKM AAVSKACGNM FGGLLICLPR
EQAARFCAEI KSPKYGEGHQ AWIIGIVEKG NRTARIIDKP RIIEVAPQVA TQNVNPTPGA
AS
//
