ID   A0A368H448_ANCCA        Unreviewed;       531 AA.
AC   A0A368H448;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=GDA1/CD39 family protein {ECO:0000313|EMBL:RCN51381.1};
GN   ORFNames=ANCCAN_02534 {ECO:0000313|EMBL:RCN51381.1};
OS   Ancylostoma caninum (Dog hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN51381.1, ECO:0000313|Proteomes:UP000252519};
RN   [1] {ECO:0000313|EMBL:RCN51381.1, ECO:0000313|Proteomes:UP000252519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Baltimore {ECO:0000313|EMBL:RCN51381.1,
RC   ECO:0000313|Proteomes:UP000252519};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Ancylostoma caninum.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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:RCN51381.1}.
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DR   EMBL; JOJR01000014; RCN51381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368H448; -.
DR   STRING; 29170.A0A368H448; -.
DR   Proteomes; UP000252519; 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   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:SF121; NUCLEOSIDE-DIPHOSPHATASE MIG-23; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU003833};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252519};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        473..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        161
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         197..201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   531 AA;  60618 MW;  C91DB0DE3D17EB7B CRC64;
     MVRMASRVLY LLLIVIVCIP LFLILNHSDH GSTITSYMQG NRHMEGIRQL ITDKELISIT
     PALDHLNNPV VKKVYPGLSS FQDNPHKAAE YVKPLLDYAS QFIPHEKLPY TPVFLLATAG
     MRLVPQKQQN AILNDLHTKL PQMTPMQIMK EHIRVIEGKW EGIYSWIAVN YILGKFKASN
     SSLSSRPDTV GMIDMGGASM QIAFEMEPKD EFRSENVENV NLGCRDDDDR YKYKLFVTTF
     LGYGVNEGLR KYEQELSDRL LHTKESYVRD ECMPVNLQKV INRSDGTMFV RKGIGDWNGC
     VKQLAELLNK PSIHPKYLCQ PKCFFGTVAA PLVSLSKMKI YGFSEYWYSL DEVLSLGGQY
     NHSLIAEKSK QYCSQRWSQI QAAARRKLYP KSNEDRLKSQ CFKSAWITAI LHDGFEVDRE
     HNKFQSAFTI AGQEVQWALG AMIYHMRYFP LKNSATNLVV NKHPHDSSLP SSFSLWLLMV
     AMVALVALFA FVTLKEDLSS GLRRNRSMWS YMMLNTSDSS SLSSFRSVSY A
//