ID M3XGN1_LATCH Unreviewed; 330 AA.
AC M3XGN1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=selenide, water dikinase {ECO:0000256|ARBA:ARBA00011997};
DE EC=2.7.9.3 {ECO:0000256|ARBA:ARBA00011997};
GN Name=SEPHS2 {ECO:0000313|Ensembl:ENSLACP00000021887.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000021887.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000021887.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AFYH01214970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01214971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01214972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01214973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006010212.1; XM_006010150.2.
DR AlphaFoldDB; M3XGN1; -.
DR Ensembl; ENSLACT00000026705.1; ENSLACP00000021887.1; ENSLACG00000005815.2.
DR GeneID; 102350406; -.
DR KEGG; lcm:102350406; -.
DR CTD; 352933; -.
DR GeneTree; ENSGT00390000000950; -.
DR HOGENOM; CLU_032859_1_0_1; -.
DR OrthoDB; 177624at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000005815; Expressed in muscle tissue and 4 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:UP000008672};
KW Selenium {ECO:0000256|ARBA:ARBA00023266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..107
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 126..299
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 311..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 330 AA; 35757 MW; A477BB7645D73C95 CRC64;
MDSCVIPLRH GGLSLVQTTD FFYPLVEDPY MMGRIACANV LSDLYAMGIT ECDNMLMLLS
VSQKMSEQER EIIMPLMIRG FRDAAEEGGT SVTGGQTVIN PWIIIGGVAT VVCQPNEFIM
PHNAIPGDVL VLTKPLGTQV AVNAHQWLEI PERWNKIKLV VSKEDVELAY QEAMLNMAML
NRTAAALMHT FNAHAATDIT GFGILGHAQN LAKEQRSEVS FVIHNLPIIA KMAAVSKACG
TVFGLLQGTS AETSGGLLIC LPREQAARFC AEVKSPKYGE GHQAWIIGIV EKGNRTARII
DKPRIIEVAP RGATASAQEN NSNASPESIS
//
