ID   ASNA_TOXGV              Reviewed;         397 AA.
AC   B9PGU1; V4ZKI3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
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=TGVEG_231190;
OS   Toxoplasma gondii (strain ATCC 50861 / VEG).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=432359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50861 / VEG;
RA   Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT   "Annotation of Toxoplasma gondii VEG.";
RL   Submitted (MAR-2008) 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; AAYL02000022; ESS35578.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9PGU1; -.
DR   SMR; B9PGU1; -.
DR   STRING; 5811.TGME49_031190; -.
DR   EnsemblProtists; ESS35578; ESS35578; TGVEG_231190.
DR   EnsemblProtists; TGME49_231190-t26_1; TGME49_231190-t26_1; TGME49_231190.
DR   VEuPathDB; ToxoDB:TGVEG_231190; -.
DR   eggNOG; KOG2825; Eukaryota.
DR   InParanoid; B9PGU1; -.
DR   Proteomes; UP000002226; Partially assembled 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: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; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00345; GET3_arsA_TRC40; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW   Nucleotide-binding; Reference proteome; Transport.
FT   CHAIN           1..397
FT                   /note="ATPase ASNA1 homolog"
FT                   /id="PRO_0000388176"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         27..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         261
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
SQ   SEQUENCE   397 AA;  44049 MW;  A077BF0B0BEF8B40 CRC64;
     MEDLELEGSL KELFETPSLR WIFVGGKGGV GKTTTSCAVA AQLAKTRESV LIISTDPAHN
     ISDAFTQKFS NTPTLVNGFD NLYAMEIDSR YQETFDFKMS NLPSAEAASF SLTSLLPEML
     QAVPGIDEAL SFAELMQNVQ SMKYSVIVFD TAPTGHTLRL LAFPDLLERG LKKLSTFKDK
     IQSALQMLNA VSGQQIQEQD FAAKIENLKA VTTSVREAFQ DPAHTTFVCV CIPEFLSVYE
     TERLVQELAK QKIDCSNIVV NQVLFPVGGV QDEGCRPPAS LLASADAETP APLEELLAPP
     AARGEKETAQ EENARLRQLI RRMQIRLLAL EKSYHSRRAM QSRYLQQIQD LYSFDFHVVP
     IPQQPEEVRG IERLLRFGDL LSSCRPLPIL PPAPSSP