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Database: UniProt
Entry: A0A1A8YMV1_9APIC
LinkDB: A0A1A8YMV1_9APIC
Original site: A0A1A8YMV1_9APIC 
ID   A0A1A8YMV1_9APIC        Unreviewed;       379 AA.
AC   A0A1A8YMV1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=ATPase ASNA1 homolog {ECO:0000256|HAMAP-Rule:MF_03112};
DE            EC=3.6.-.- {ECO:0000256|HAMAP-Rule:MF_03112};
DE   AltName: Full=Arsenical pump-driving ATPase homolog {ECO:0000256|HAMAP-Rule:MF_03112};
DE   AltName: Full=Arsenite-stimulated ATPase {ECO:0000256|HAMAP-Rule:MF_03112};
GN   ORFNames=POVWA2_012110 {ECO:0000313|EMBL:SBT32918.1};
OS   Plasmodium ovale wallikeri.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=864142 {ECO:0000313|EMBL:SBT32918.1, ECO:0000313|Proteomes:UP000078550};
RN   [1] {ECO:0000313|Proteomes:UP000078550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Naeem Raeece;
RL   Submitted (MAY-2016) 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:0000256|HAMAP-Rule:MF_03112}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03112}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03112}.
CC       Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03112}.
CC   -!- SIMILARITY: Belongs to the arsA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00011040, ECO:0000256|HAMAP-Rule:MF_03112}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03112}.
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DR   EMBL; FLRE01000046; SBT32918.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A8YMV1; -.
DR   Proteomes; UP000078550; 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   CDD; cd02035; ArsA; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00345; GET3_arsA_TRC40; 1.
DR   PANTHER; PTHR10803; ARSENICAL PUMP-DRIVING ATPASE ARSENITE-TRANSLOCATING ATPASE; 1.
DR   PANTHER; PTHR10803:SF3; ATPASE GET3; 1.
DR   Pfam; PF02374; ArsA_ATPase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03112};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03112};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW   Rule:MF_03112}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_03112};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03112};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_03112}.
FT   DOMAIN          42..309
FT                   /note="Anion-transporting ATPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02374"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         49..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT   BINDING         276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
SQ   SEQUENCE   379 AA;  43102 MW;  0D56BF5EDDC0AFFB CRC64;
     MSGEEEISSS SSSCSLSLES DSYNEEDYET NLTKLIENKT LNWIFVGGKG GVGKTTTSCS
     IAIQLAKKRE SVLLLSTDPA HNTSDAFNQK FTNKPTLIKP YTNLYCMEID TTYSENTAFK
     LNKTEFLDNI IPELLQSFPG IDEALCFAEL MQSIKNMEYS VIVFDTAPTG HTLRLLAFPE
     LLKKALGYII NLREKLKGTL NMLKNLTNNE MELDGLYDKI NHLNAMSISI QANFQNPLKT
     TFVCVCIPEF LSVYETERLI QELTKKNISC YNIVVNQVVF PLDSQHVDLT NCETMLKQIN
     DKNIQNVFNS LISKTKELED VYISRRKLQS KYLTQIKNLY GNDFHIVCMP QLKSEIRGLE
     NISSFSEMLL QSKEIPIYK
//
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