ID   ASNA_CRYPI              Reviewed;         366 AA.
AC   A3FPQ6;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, 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   ORFNames=cgd7_4070;
OS   Cryptosporidium parvum (strain Iowa II).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=353152;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa II;
RX   PubMed=15044751; DOI=10.1126/science.1094786;
RA   Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA   Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA   Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA   Anantharaman V., Aravind L., Kapur V.;
RT   "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL   Science 304:441-445(2004).
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; AAEE01000001; EAZ51595.1; -; Genomic_DNA.
DR   RefSeq; XP_001388402.1; XM_001388365.1.
DR   AlphaFoldDB; A3FPQ6; -.
DR   SMR; A3FPQ6; -.
DR   STRING; 353152.A3FPQ6; -.
DR   EnsemblProtists; EAZ51595; EAZ51595; cgd7_4070.
DR   GeneID; 3371804; -.
DR   KEGG; cpv:cgd7_4070; -.
DR   InParanoid; A3FPQ6; -.
DR   OMA; TTVSCAY; -.
DR   Proteomes; UP000006726; Chromosome 7.
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; 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;
KW   Nucleotide-binding; Reference proteome; Transport.
FT   CHAIN           1..366
FT                   /note="ATPase ASNA1 homolog"
FT                   /id="PRO_0000388166"
FT   ACT_SITE        62
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT   BINDING         33..40
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   366 AA;  40886 MW;  F1FCC2E2BDE1CECC CRC64;
     MSTAYFDADC DLEPSLKSLF SLKTLKWIFV GGKGGVGKTT TSCSIASRLA EERESVLILS
     TDPAHNLSDA FVQKFSNAPT LVNGYKNLYA MELDASYQQA VEFKLKEENS LFSKFLPDLI
     SALPGIDEAL GFATLMQSVK SMSYSVIVFD TAPTGHTLRL LSFPSLLEKG LSKLFSIKQN
     MSGALQLINS VSGNAIEEET LNSKLEDLKA ITTSVKETFQ DPSKTTFVCV CIPEFLSVYE
     TERLIQELAK QSISCSHIVV NQVMFPIDLP SGNDQGESVL KDSSELLKLE DIPSDHSKLV
     EFTEKIVCSY NKLLSYSKLL YSKYYSKRNM QMKYLEQIRD LYSYDFHVAY IPTLNNEVSK
     IRVLIS