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}.
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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
//