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Database: UniProt
Entry: G3PII2_GASAC
LinkDB: G3PII2_GASAC
Original site: G3PII2_GASAC 
ID   G3PII2_GASAC            Unreviewed;       382 AA.
AC   G3PII2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=selenide, water dikinase {ECO:0000256|ARBA:ARBA00011997};
DE            EC=2.7.9.3 {ECO:0000256|ARBA:ARBA00011997};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000017410.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000017410.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000017410.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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};
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DR   AlphaFoldDB; G3PII2; -.
DR   STRING; 69293.ENSGACP00000017410; -.
DR   Ensembl; ENSGACT00000017444.1; ENSGACP00000017410.1; ENSGACG00000013165.1.
DR   eggNOG; KOG3939; Eukaryota.
DR   GeneTree; ENSGT00390000000950; -.
DR   InParanoid; G3PII2; -.
DR   OMA; LDQSERW; -.
DR   TreeFam; TF313811; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000013165; Expressed in embryo and 13 other cell types or tissues.
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:SF1; SELENIDE, WATER DIKINASE 2; 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   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
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          176..350
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   REGION          363..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   382 AA;  40906 MW;  983B7CE7E04B58D4 CRC64;
     GCKVPQEALL KLLAGLEADR ADGDREGRRP SVRLRPTAAR PSTRLLAGVG MDCCVIPLRH
     GGLSLVQTTD FFYPLVEDPY MMGRIACANV LSDLYAMGIT ECDNMLMLLS VSQKMNDKDR
     ERVMPLIIQG FRDAAEEGGT SVTGGQTVIN PWIIVGGVAS VVCQPNEFIM PDGAVPGDVL
     VLTKPLGTQV AVNAHQWLDQ TERWNKIKLV VTKEEVKEAY QEAMFSMATL NRTAAGLMHK
     FQAHAATDVT GFGLLGHANN LAAQQRDEVA FVIHNLPIIA KMAAISKACG NLFNLIQGTS
     AETSGGLLVC LPREQAAKFC SEMKSQSSAA GGQGAAGGAW IIGIVEKGDR RARIIDKPRI
     IEVPARGSQT ANQENNSASP SP
//
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