ID   A0A3B0K8L2_DROGU        Unreviewed;       464 AA.
AC   A0A3B0K8L2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Blast:Ectonucleoside triphosphate diphosphohydrolase 5 {ECO:0000313|EMBL:SPP82389.1};
GN   ORFNames=DGUA_6G014253 {ECO:0000313|EMBL:SPP82389.1};
OS   Drosophila guanche (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP82389.1, ECO:0000313|Proteomes:UP000268350};
RN   [1] {ECO:0000313|Proteomes:UP000268350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; OUUW01000006; SPP82389.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0K8L2; -.
DR   Proteomes; UP000268350; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF83; NTPASE, ISOFORM F; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Hydrolase {ECO:0000313|EMBL:SPP82389.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         232..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   464 AA;  51228 MW;  E56051412E3E50CA CRC64;
     MTSTDVRKRK LATDEKPLQG NRRKGSSSVS GSRGPSGLKI SFLCLIVSVV LLLFVFGFVS
     ENASPYLARL ASKFGYSKVQ YAAIIDAGST GSRVLAYKFN RSFIDNKLVL YEELFKERKP
     GLSSFADNPA EGAHSIKLLL DEARAFIPKE HWSSTPLVLK ATAGLRLLPQ SKAENILNAV
     RDLFAKSEFS VDMDAVEIMD GTDEGIFSWF TVNFLLGRLS KTNQAAALDL GGGSTQVTFS
     PTDPEQVPVY DKYMHEVVTS SKKINVFTHS YLGLGLMAAR HAVFTHGHKK EDTLLESVCV
     NPIIANRTWT YGNVQYKVSG RDNTKSSAAE QPIVDFEACL ELVKSKVMPL VKPKPFTLKQ
     HAVAAFSYYF ERAIESGLVD PLAGGETTVE AYRKKAQEIC AIPNDEQPFM CFDLTFISTL
     LREGFGLNDG KKIKLYKKID GHEISWALGC AYNVLTSDEK FSNS
//