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Database: UniProt
Entry: A0A9W7L009_9STRA
LinkDB: A0A9W7L009_9STRA
Original site: A0A9W7L009_9STRA 
ID   A0A9W7L009_9STRA        Unreviewed;       803 AA.
AC   A0A9W7L009;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   28-JAN-2026, entry version 10.
DE   RecName: Full=Selenide, water dikinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TrLO_g7035 {ECO:0000313|EMBL:GMI18227.1};
OS   Triparma laevis f. longispina.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bolidophyceae; Parmales;
OC   Triparmaceae; Triparma.
OX   NCBI_TaxID=1714387 {ECO:0000313|EMBL:GMI18227.1, ECO:0000313|Proteomes:UP001165122};
RN   [1] {ECO:0000313|Proteomes:UP001165122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES 3700 {ECO:0000313|Proteomes:UP001165122};
RX   PubMed=37420035; DOI=10.1038/s42003-023-05002-x;
RA   Ban H., Sato S., Yoshikawa S., Yamada K., Nakamura Y., Ichinomiya M.,
RA   Sato N., Blanc-Mathieu R., Endo H., Kuwata A., Ogata H.;
RT   "Genome analysis of Parmales, the sister group of diatoms, reveals the
RT   evolutionary specialization of diatoms from phago-mixotrophs to
RT   photoautotrophs.";
RL   Commun. Biol. 6:0-0(2023).
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:GMI18227.1}.
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DR   EMBL; BRXW01000327; GMI18227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9W7L009; -.
DR   OrthoDB; 409395at2759; -.
DR   Proteomes; UP001165122; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0004756; F:selenide, water dikinase activity; IEA:TreeGrafter.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd02195; SelD; 1.
DR   Gene3D; 3.50.50.100; -; 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; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
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; IPR017584; Pyridine_nucleo_diS_OxRdtase_N.
DR   InterPro; IPR004536; SPS/SelD.
DR   NCBIfam; TIGR03169; Nterm_to_SelD; 1.
DR   NCBIfam; TIGR00476; selD; 1.
DR   PANTHER; PTHR10256:SF0; INACTIVE SELENIDE, WATER DIKINASE-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10256; SELENIDE, WATER DIKINASE; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP001165122};
KW   Selenium {ECO:0000256|ARBA:ARBA00023266};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..321
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          477..586
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          655..779
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   803 AA;  86459 MW;  9D50CCF1D0B46E23 CRC64;
     MDATPLYSDL VLIGGGHAHV NLLKMYGMEE YKDRLKGIRL TLITRDVSTP YSGMLPGYVS
     GHYTHEQCHL DLSLLCSHSG FRLIHASATG IEINESGKGG SVTVDDGRPP IRFDALSVDI
     GSSPQYCSTG SSHITPVKPI DGFAHRWSSL VDRVSSDVSN EIIKVAVVGG GAGGIELTLA
     INERLKKIVK GEGRVEVTVF NRGGEILQQH NPKVREIFDR ILKERNVHVV RNATATSVTA
     STSNSNTKTL HYTHNDTPTS SLFSEIIWCT SASSQPWLRT SAPFETTDDG FILVDDMFQT
     SIPGIFAAGD CCHNRSGSRP KAGVFAVRAG PILRDNMLNF LMGNKLIEYV LQKEFLGLIS
     TGDKYAVASR GSFALEGAFL WKLKDEIDVK WMKSYKELPE MKVELDFPEI AQSKGAVAMA
     AFAEAPMRCG GCGAKVGAST LSRVLKAVRE RRHLQEQNAS PNPNPNSSIP TSLSSMDDCA
     VCPPPPRDCM TVHTIDFFRS FISDPFIFGR ISAVHSLSDC HAMGALPQTA LALAVAPYAV
     TESITEDTLI AMLSGASDAL FEEGCALAGG HTCEGAELSL GFAVNGYLPP NFPGFLKAGG
     QPTNKIVLTK RVGTGALFAA EMRGKVNGIF RTEAINEMCK SNGRAAKIIT DPQFVESVKA
     VTDVTGFGLV GHLLEMLDYE AGIGAKLEIS KIPFFDGAVS AAKQNIYSSL QKSNENSRRA
     VKNHIVVAKT HPEKSRLLYD PQTAGGLLII MEAEMAEALV SSMKDSGYDN CAVIGEIVAI
     EKPSANGGEE DSCVLRKLVE VVE
//
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