ID   A0A1A8W0D6_9APIC        Unreviewed;       567 AA.
AC   A0A1A8W0D6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Adenosine-diphosphatase, putative {ECO:0000313|EMBL:SBS86225.1};
GN   ORFNames=POVCU2_0035950 {ECO:0000313|EMBL:SBS86225.1};
OS   Plasmodium ovale curtisi.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=864141 {ECO:0000313|EMBL:SBS86225.1, ECO:0000313|Proteomes:UP000078560};
RN   [1] {ECO:0000313|Proteomes:UP000078560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Naeem Raeece;
RL   Submitted (MAY-2016) 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; FLQU01000479; SBS86225.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A8W0D6; -.
DR   Proteomes; UP000078560; 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:InterPro.
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:SF128; PUTATIVE-RELATED; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078560};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          427..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..447
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         245..249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   567 AA;  65991 MW;  90E3F604977E4251 CRC64;
     MKNEKITRKE SLIFIAFLWV LFLCLNLRVN CEKVRKLNEG EKEEIDNSTI HKCVVIDAGS
     TGTRVYIYNY KITNDDKEMK IYIPAISYRT TPGLVYILND YFSNGEEKSF YDYFNNIKSF
     IYNNVLEEER ETTFILLRAS GGFRLLSINK SEKYINFVKN YFLKNFNEFL LIDDFLVKVL
     SGKEEAILSF VSIYALLGKF SPNPLIFTDQ GEDDGTIGSV EEESKGESIP LDQDDDSIGV
     LELGGATAQV IIKIPMSKMN EDILNLFNYQ HKENKKKGII EENYKNKNIV KIHFCNKDIY
     LYCKSYLVLG RQNAMKTYLH YIVHENSKKD NTMNKYMHVA CFPKDFKFYI NNLYKTSIEE
     EIQEYNDNTQ LGEYEFVGIG TGDIDLCRTQ IQNILTHAQI DILPFKLKKF IKLYGIENFH
     HFAIVRGAKK KQKTKNKKQK KNKKQKQEQK QKHEQKHEQK QKQKKYMSVA RRPFGCYHIR
     HIEPPGNAQP NFAEHEHVPG KGERDLPPHD RRNKEGGQAR LEHRKGADFL LWVSTGGHLD
     EDAADFSATC RCRISHDGPF HFPPVHG
//