ID A0A0A0ADQ1_CHAVO Unreviewed; 393 AA.
AC A0A0A0ADQ1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=N301_07922 {ECO:0000313|EMBL:KGL91603.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL91603.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL91603.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL91603.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KL871261; KGL91603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0ADQ1; -.
DR STRING; 50402.A0A0A0ADQ1; -.
DR Proteomes; UP000053858; 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:KGL91603.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW Selenium {ECO:0000256|ARBA:ARBA00023266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 70..175
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 194..367
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL91603.1"
FT NON_TER 393
FT /evidence="ECO:0000313|EMBL:KGL91603.1"
SQ SEQUENCE 393 AA; 42995 MW; 23C0BDF9584DB1A1 CRC64;
TMSVRESFNP ESYELDESFR LTRFAELKGT GCKVPQDVLQ KLLESLQENH FQEDEQFLGA
VMPRLGIGMD TCVIPLRHGG LSLVQTTDYI YPIVDDPYMM GRIACANVLS DLYAMGVTEC
DNMLMLLGIS NKMTDRERDK VMPLIIQGFK DAAEEAGTSV TGGQTVLNPW IVLGGVATTV
CQPNEFIMPD NAVPGDVLVL TKPLGTQVAV AVHQWLDIPE KWNKIKLVVT QEDVELAYQE
AMMNMARLNR TAAGLMHTFN AHAATDITGF GILGHAQNLA KQQRNEVSFV IHNLPVLAKM
AAVSKACGNM FGLMHGTCPE TSGGLLICLP REQAARFCAE IKSPKYGEGH QAWIIGIVEK
GNRTARIIDK PRIIEVAPQV ATQNVNPTPG ATS
//
