ID   ASNA_BABBO              Reviewed;         358 AA.
AC   A7AW49;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=BBOV_I001930;
OS   Babesia bovis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=5865;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T2Bo;
RX   PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
RA   Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
RA   Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
RA   Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H.,
RA   Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr.,
RA   Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F.,
RA   Nene V.M.;
RT   "Genome sequence of Babesia bovis and comparative analysis of apicomplexan
RT   hemoprotozoa.";
RL   PLoS Pathog. 3:1401-1413(2007).
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; AAXT01000005; EDO05277.1; -; Genomic_DNA.
DR   RefSeq; XP_001608845.1; XM_001608795.1.
DR   AlphaFoldDB; A7AW49; -.
DR   SMR; A7AW49; -.
DR   STRING; 5865.XP_001608845.1; -.
DR   EnsemblProtists; EDO05277; EDO05277; BBOV_I001930.
DR   GeneID; 5477061; -.
DR   KEGG; bbo:BBOV_I001930; -.
DR   VEuPathDB; PiroplasmaDB:BBOV_I001930; -.
DR   eggNOG; KOG2825; Eukaryota.
DR   InParanoid; A7AW49; -.
DR   Proteomes; UP000002173; 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..358
FT                   /note="ATPase ASNA1 homolog"
FT                   /id="PRO_0000388165"
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         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
SQ   SEQUENCE   358 AA;  40565 MW;  41C27297048EB8AB CRC64;
     MVEITEVIEP EWQTRNDIQN LVNQKTLQWV FVGGKGGVGK TTISSSIATA LAETRESVLL
     LSTDPAHSLS DAFGQKFTHE PRLVNGFTNL YAMELNTSQI IDGLDGLRET HSFLKNVPDI
     LMMLPGIDEA LSFVELMQSV QSRRFSVTIF DTAPTGHTLK FLKLPDVLEK ILDSLLKLEN
     TMGGLLQLFS SMTKAQMSQN ELFDKIKLLG DMINTTHEQM KNPDLTTFIC VCIPEFLSVY
     ETERLIQDLA KSEIDCSYII VNQVLKHIQL GGLIEDAWDG LTEEQQRIMT PFFEKVREHH
     STHNSRVDVQ RKYLSDIKDL YQEDFNIVAV HQNKQEVRGK DALVAFAKKL MQHSPLPI