ID A0A498L5L4_LABRO Unreviewed; 391 AA.
AC A0A498L5L4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=selenide, water dikinase {ECO:0000256|ARBA:ARBA00011997};
DE EC=2.7.9.3 {ECO:0000256|ARBA:ARBA00011997};
GN ORFNames=ROHU_020973 {ECO:0000313|EMBL:RXN26039.1}, ROHU_034889
GN {ECO:0000313|EMBL:RXN02713.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN02713.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN02713.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN02713.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN02713.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) 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 -!- 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:RXN02713.1}.
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DR EMBL; QBIY01013496; RXN02713.1; -; Genomic_DNA.
DR EMBL; QBIY01012243; RXN26039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498L5L4; -.
DR STRING; 84645.A0A498L5L4; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RXN02713.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498L5L4};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Selenium {ECO:0000256|ARBA:ARBA00023266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 48..152
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 172..324
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 41729 MW; 01A1557B62EC69C3 CRC64;
MLKLLQGLEP DRPPGEDGGS GTGVGDETNE FGQLVSVAHG PRLGIGMDSC VIPLRHGGLS
LVQTTDFFYP LVEDPYMMGR IACANVLSDL YAMGITECDN MLMLLSVSQK MNEKERDQVI
PLMMKGFRDA AEEAGTSVTG GQTVVNPWII IGGVASVVCQ PNDFIMPDSA VPGDVLVLTK
PLGTQVAVNA HQWLDIPEKW NKIKLVISRE EVEQAYQEAM LNMATLNRTA AALMHKFNAH
AATDITGFGI IGHARNLAQQ QKNDVAFVIH NLPIISKMAA ISKAGGNLFG LLHGTSSETS
GGLLICLPRE QAARFCAEMK SSRVGLSGAV GQDGGAGDGQ QAWIIGIVEK GNRCARIIDK
PRIIEVPYRG SVVSAQEGSN NNASPPEVQL T
//