ID A0A0L1IHW4_PLAFA Unreviewed; 379 AA.
AC A0A0L1IHW4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=PFMG_04939 {ECO:0000313|EMBL:KNG78778.1};
OS Plasmodium falciparum IGH-CR14.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=580059 {ECO:0000313|EMBL:KNG78778.1, ECO:0000313|Proteomes:UP000054562};
RN [1] {ECO:0000313|Proteomes:UP000054562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGH-CR14 {ECO:0000313|Proteomes:UP000054562};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "Annotation of Plasmodium falciparum IGH-CR14.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGH-CR14 {ECO:0000313|Proteomes:UP000054562};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Godfrey P., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Wirth D.F., Nusbaum C., Birren B.;
RT "The genome sequence of Plasmodium falciparum IGH-CR14.";
RL Submitted (JUL-2015) 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; GG665716; KNG78778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L1IHW4; -.
DR SMR; A0A0L1IHW4; -.
DR EnsemblProtists; KNG78778; KNG78778; PFMG_04939.
DR Proteomes; UP000054562; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000054562};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_03112}.
FT DOMAIN 39..309
FT /note="Anion-transporting ATPase-like"
FT /evidence="ECO:0000259|Pfam:PF02374"
FT DOMAIN 317..367
FT /note="Anion-transporting ATPase-like"
FT /evidence="ECO:0000259|Pfam:PF02374"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 75
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
FT BINDING 273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03112"
SQ SEQUENCE 379 AA; 43317 MW; C5596A0736EA59CB CRC64;
MSEDESNSVS CSLSLESDGY SDEEYDTNLN KLIENESLNW IFVGGKGGVG KTTTSCSIAV
QLSKRRESVL LLSTDPAHNT SDAFNQKFTN QPTLINSFDN LYCMEIDTNY SENTAFKLNK
KEMFDNILPE LLHSFPGIDE ALCFAELMQS IKNMKYSVIV FDTAPTGHTL RLLAFPDLLK
KALGYLINIR EKLKGTLNVL KNFTNNEMEF DSLYEKINHL NAMSSSIQAN FQNPMKTTFV
CVCIPEFLSV YETERLIQEL TKKNISCYNI VVNQVVFPLD SPNVNLENCK NLLSQIKNEQ
IQSYFNDLIS KTEELEDVYI SRRKLQSKYL TQIKNLYSND FHIVCMPQLK NEIRGLNNIS
SFSEMLLQSK DIPIYKDNL
//
