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Selenide, water dikinase (EC 2.7.9.3) (Protein patufet) (Selenium donor protein) (Selenophosphate synthase) (dSelD)

 SPS1_DROME              Reviewed;         398 AA.
O18373; O18597; Q0E979; Q9V700;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
12-SEP-2018, entry version 145.
RecName: Full=Selenide, water dikinase;
EC=2.7.9.3;
AltName: Full=Protein patufet;
AltName: Full=Selenium donor protein;
AltName: Full=Selenophosphate synthase;
AltName: Full=dSelD;
Name=SelD; Synonyms=PTF1, ptuf; ORFNames=CG8553;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Canton-S; TISSUE=Embryo;
PubMed=9398525; DOI=10.1006/jmbi.1997.1371;
Persson B.C., Boeck A., Jaeckle H., Vorbrueggen G.;
"SelD homolog from Drosophila lacking selenide-dependent
monoselenophosphate synthetase activity.";
J. Mol. Biol. 274:174-180(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=9491069; DOI=10.1007/s004380050630;
Alsina B., Serras F., Baguna J., Corominas M.;
"patufet, the gene encoding the Drosophila melanogaster homologue of
selenophosphate synthetase, is involved in imaginal disc
morphogenesis.";
Mol. Gen. Genet. 257:113-123(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10444382;
Alsina B., Corominas M., Berry M.J., Baguna J., Serras F.;
"Disruption of selenoprotein biosynthesis affects cell proliferation
in the imaginal discs and brain of Drosophila melanogaster.";
J. Cell Sci. 112:2875-2884(1999).
[7]
FUNCTION.
PubMed=11258485; DOI=10.1093/embo-reports/kvd087;
Hirosawa-Takamori M., Jackle H., Vorbruggen G.;
"The class 2 selenophosphate synthetase gene of Drosophila contains a
functional mammalian-type SECIS.";
EMBO Rep. 1:441-446(2000).
-!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
Essential for progression of the cell cycle by controlling the
synthesis of selenoproteins. Plays a role in apoptosis and
consequently a role in imaginal disk patterning and growth.
{ECO:0000269|PubMed:10444382, ECO:0000269|PubMed:11258485,
ECO:0000269|PubMed:9398525, ECO:0000269|PubMed:9491069}.
-!- CATALYTIC ACTIVITY: ATP + selenide + H(2)O = AMP + selenophosphate
+ phosphate.
-!- TISSUE SPECIFICITY: Expressed at low levels throughout the embryo.
At later developmental stages, expressed in areas of high cell
proliferation. From embryo stage 13, expression is high in central
nervous system and midgut, especially in the gastric caeca.
Expression also seen in larval imaginal disks and brain.
{ECO:0000269|PubMed:10444382, ECO:0000269|PubMed:9398525,
ECO:0000269|PubMed:9491069}.
-!- DEVELOPMENTAL STAGE: Throughout development, from embryo to adult.
{ECO:0000269|PubMed:9491069}.
-!- SIMILARITY: Belongs to the selenophosphate synthase 1 family.
Class II subfamily. {ECO:0000305}.
-!- CAUTION: The conserved active site Cys (or selenocysteine) residue
in position 49 is replaced by an Arg. However, as function in
selenoprotein synthesis is proven, it is possible Cys-51 is the
active site. {ECO:0000305}.
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EMBL; AJ000672; CAA04229.1; -; mRNA.
EMBL; U91994; AAB88790.1; -; Genomic_DNA.
EMBL; AE013599; AAF58266.1; -; Genomic_DNA.
EMBL; AY095058; AAM11386.1; -; mRNA.
RefSeq; NP_725374.1; NM_166045.2.
RefSeq; NP_725375.1; NM_166046.2.
UniGene; Dm.2979; -.
ProteinModelPortal; O18373; -.
SMR; O18373; -.
BioGrid; 62337; 12.
DIP; DIP-21887N; -.
IntAct; O18373; 6.
STRING; 7227.FBpp0086691; -.
PaxDb; O18373; -.
PRIDE; O18373; -.
EnsemblMetazoa; FBtr0087564; FBpp0086690; FBgn0261270.
EnsemblMetazoa; FBtr0087565; FBpp0086691; FBgn0261270.
GeneID; 36587; -.
KEGG; dme:Dmel_CG8553; -.
CTD; 36587; -.
FlyBase; FBgn0261270; SelD.
eggNOG; KOG3939; Eukaryota.
eggNOG; COG0709; LUCA.
GeneTree; ENSGT00390000000950; -.
InParanoid; O18373; -.
KO; K01008; -.
OMA; GCIPGGT; -.
OrthoDB; EOG091G0B7N; -.
PhylomeDB; O18373; -.
Reactome; R-DME-2408557; Selenocysteine synthesis.
GenomeRNAi; 36587; -.
PRO; PR:O18373; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0261270; Expressed in 39 organ(s), highest expression level in embryo.
Genevisible; O18373; DM.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IMP:FlyBase.
GO; GO:0006541; P:glutamine metabolic process; IMP:FlyBase.
GO; GO:0007444; P:imaginal disc development; IMP:FlyBase.
GO; GO:0007005; P:mitochondrion organization; IMP:FlyBase.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:FlyBase.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:FlyBase.
GO; GO:0016260; P:selenocysteine biosynthetic process; IMP:FlyBase.
CDD; cd02195; SelD; 1.
Gene3D; 3.30.1330.10; -; 1.
Gene3D; 3.90.650.10; -; 2.
InterPro; IPR010918; PurM-like_C_dom.
InterPro; IPR036676; PurM-like_C_sf.
InterPro; IPR016188; PurM-like_N.
InterPro; IPR036921; PurM-like_N_sf.
InterPro; IPR023061; SelD_I.
InterPro; IPR004536; SPS/SelD.
PANTHER; PTHR10256; PTHR10256; 1.
Pfam; PF00586; AIRS; 1.
Pfam; PF02769; AIRS_C; 1.
PIRSF; PIRSF036407; Selenphspht_syn; 1.
SUPFAM; SSF55326; SSF55326; 1.
SUPFAM; SSF56042; SSF56042; 1.
TIGRFAMs; TIGR00476; selD; 1.
2: Evidence at transcript level;
ATP-binding; Cell cycle; Complete proteome; Developmental protein;
Kinase; Nucleotide-binding; Reference proteome; Selenium; Transferase.
CHAIN 1 398 Selenide, water dikinase.
/FTId=PRO_0000127652.
NP_BIND 290 296 ATP. {ECO:0000255}.
ACT_SITE 51 51 {ECO:0000255}.
SITE 52 52 Important for catalytic activity.
{ECO:0000250}.
CONFLICT 253 254 ED -> KN (in Ref. 2; AAB88790).
{ECO:0000305}.
SEQUENCE 398 AA; 43446 MW; B265DAF4FDACC2D8 CRC64;
MSYAADVLNS AHLELHGGGD AELRRPFDPT AHDLDASFRL TRFADLKGRG CKVPQDVLSK
LVSALQQDYS AQDQEPQFLN VAIPRIGIGL DCSVIPLRHG GLCLVQTTDF FYPIVDDPYM
MGKIACANVL SDLYAMGVTD CDNMLMLLAV STKMTEKERD VVIPLIMRGF KDSALEAGTT
VTGGQSVVNP WCTIGGVAST ICQPNEYIVP DNAVVGDVLV LTKPLGTQVA VNAHQWIDQP
ERWNRIKLVV SEEDVRKAYH RAMNSMARLN RVAARLMHKY NAHGATDITG FGLLGHAQTL
AAHQKKDVSF VIHNLPVIAK MAAVAKACGN MFQLLQGHSA ETSGGLLICL PREQAAAYCK
DIEKQEGYQA WIIGIVEKGN KTARIIDKPR VIEVPAKD


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