ID   ASNA_THEPA              Reviewed;         361 AA.
AC   Q4N0J4;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
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   OrderedLocusNames=TP03_0142;
OS   Theileria parva (East coast fever infection agent).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5875;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Muguga;
RX   PubMed=15994558; DOI=10.1126/science.1110439;
RA   Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA   Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA   Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA   Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA   Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA   Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA   Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA   Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT   "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT   lymphocytes.";
RL   Science 309:134-137(2005).
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; AAGK01000005; EAN30877.1; -; Genomic_DNA.
DR   RefSeq; XP_763160.1; XM_758067.1.
DR   AlphaFoldDB; Q4N0J4; -.
DR   SMR; Q4N0J4; -.
DR   STRING; 5875.XP_763160.1; -.
DR   EnsemblProtists; EAN30877; EAN30877; TP03_0142.
DR   GeneID; 3500397; -.
DR   KEGG; tpv:TP03_0142; -.
DR   VEuPathDB; PiroplasmaDB:TpMuguga_03g00142; -.
DR   eggNOG; KOG2825; Eukaryota.
DR   InParanoid; Q4N0J4; -.
DR   OMA; MDAPYEF; -.
DR   Proteomes; UP000001949; 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: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..361
FT                   /note="ATPase ASNA1 homolog"
FT                   /id="PRO_0000388175"
FT   ACT_SITE        64
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         35..42
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   361 AA;  41020 MW;  15438384038CD72E CRC64;
     MEESSMESDN GLNLRNDVKN LVEQETYKWI FVGGKGGVGK TTISCSLSSI LSERRESVLL
     LSTDPAHSLS DAFNQKFTDT PTLVNGYENL YAMELDVTRV ADTGFGLNET KMFLQTIPEL
     FQMLPGIDEA LSFSELLQSV QSMKYSVIVF DTAPTGHTLK FLNLPDTLDK LLESFLKVES
     LCGVAMKLFS ALNNSLPKEE IFQKLKRFKS NLTLIMNQMK DPNRTTFVCV CIPEFLSVYE
     TERLIQSLAK TDIDCSYIIV NQVLSYINLE EHVKNTQNSL ENLSPENKKV LDCFFELVLE
     QQNNLNGRLS IQRKYIEDIK QLYEGFFNIV AIKQYKYEVR GSEAIKEFSK ALLKHSPIPD
     S