ID   ASNA_ENTDS              Reviewed;         327 AA.
AC   B0EHY7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=ATPase ASNA1 homolog {ECO:0000255|HAMAP-Rule:MF_03112};
DE            EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_03112};
DE   AltName: Full=Arsenical pump-driving ATPase homolog {ECO:0000255|HAMAP-Rule:MF_03112};
DE   AltName: Full=Arsenite-stimulated ATPase {ECO:0000255|HAMAP-Rule:MF_03112};
GN   ORFNames=EDI_044870;
OS   Entamoeba dispar (strain ATCC PRA-260 / SAW760).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC PRA-260 / SAW760;
RA   Lorenzi H., Inman J., Schobel S., Amedeo P., Caler E.;
RT   "Annotation of Entamoeba dispar SAW760.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATPase required for the post-translational delivery of tail-
CC       anchored (TA) proteins to the endoplasmic reticulum. Recognizes and
CC       selectively binds the transmembrane domain of TA proteins in the
CC       cytosol. This complex then targets to the endoplasmic reticulum by
CC       membrane-bound receptors, where the tail-anchored protein is released
CC       for insertion. This process is regulated by ATP binding and hydrolysis.
CC       ATP binding drives the homodimer towards the closed dimer state,
CC       facilitating recognition of newly synthesized TA membrane proteins. ATP
CC       hydrolysis is required for insertion. Subsequently, the homodimer
CC       reverts towards the open dimer state, lowering its affinity for the
CC       membrane-bound receptor, and returning it to the cytosol to initiate a
CC       new round of targeting. {ECO:0000255|HAMAP-Rule:MF_03112}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03112}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112}.
CC       Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03112}.
CC   -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_03112}.
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DR   EMBL; DS549356; EDR25931.1; -; Genomic_DNA.
DR   RefSeq; XP_001737840.1; XM_001737788.1.
DR   AlphaFoldDB; B0EHY7; -.
DR   SMR; B0EHY7; -.
DR   STRING; 46681.XP_001737840.1; -.
DR   EnsemblProtists; EDR25931; EDR25931; EDI_044870.
DR   GeneID; 5882894; -.
DR   KEGG; edi:EDI_044870; -.
DR   VEuPathDB; AmoebaDB:EDI_044870; -.
DR   eggNOG; KOG2825; Eukaryota.
DR   OMA; MDAPYEF; -.
DR   OrthoDB; 992208at2759; -.
DR   Proteomes; UP000008076; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03112; Asna1_Get3; 1.
DR   InterPro; IPR025723; Anion-transp_ATPase-like_dom.
DR   InterPro; IPR016300; ATPase_ArsA/GET3.
DR   InterPro; IPR027542; ATPase_ArsA/GET3_euk.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10803; PTHR10803; 1.
DR   Pfam; PF02374; ArsA_ATPase; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00345; GET3_arsA_TRC40; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Endoplasmic reticulum; Hydrolase; Metal-binding;
KW   Nucleotide-binding; Transport; Zinc.
FT   CHAIN           1..327
FT                   /note="ATPase ASNA1 homolog"
FT                   /id="PRO_0000388163"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         265
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         277
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
SQ   SEQUENCE   327 AA;  36224 MW;  6EF4811DA1A3DC9B CRC64;
     MSLSPPNNLE HIITSQTLKW VFVGGKGGVG KTTTSCSLGV LIANRNPQKK VLIISTDPAH
     NTSDAFDIKF GAEPKAVPGV PNLSVMEVDV KDAMKGMFDG VEQGTNQNGE FGLLSEITGM
     VGMFKSVPGI DEAIAFSKII NQAQQMNYDL VLFDTAPTGH TLRFLSLPSV LRDMLEKVIK
     LQELFGPMMS QFGGIIGTNI NFNELKPKME DMLKTSEQIV KDFTNPNLTT FIPVLIPEFL
     PLYETERLIQ ELMNLNMDVN SIIVNQILPV NDCCDYCKNK RSVQAKYLGQ IDVLYSDFHL
     IKINMQTNEV RGVPALCAFS KNFEAKH