ASNA_PLAKH
ID ASNA_PLAKH Reviewed; 377 AA.
AC B3L1G8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=PKH_051870;
OS Plasmodium knowlesi (strain H).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H;
RX PubMed=18843368; DOI=10.1038/nature07306;
RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R.D., Jackson A.P.,
RA Mourier T., Mistry J., Pasini E.M., Aslett M.A., Balasubrammaniam S.,
RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA Chillingworth T., Clark T.G., Galinski M.R., Hall N., Harper D., Harris D.,
RA Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S., Marti M.,
RA Moule S., Meyer I.M., Ormond D., Peters N., Sanders M., Sanders S.,
RA Sargeant T.J., Simmonds M., Smith F., Squares R., Thurston S., Tivey A.R.,
RA Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A., Cowman A.F.,
RA Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W., Newbold C.I.,
RA Barrell B.G., Berriman M.;
RT "The genome of the simian and human malaria parasite Plasmodium knowlesi.";
RL Nature 455:799-803(2008).
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; AM910987; CAQ38737.1; -; Genomic_DNA.
DR RefSeq; XP_002258200.1; XM_002258164.1.
DR AlphaFoldDB; B3L1G8; -.
DR SMR; B3L1G8; -.
DR STRING; 5851.B3L1G8; -.
DR EnsemblProtists; CAQ38737; CAQ38737; PKH_051870.
DR GeneID; 7319588; -.
DR KEGG; pkn:PKNH_0506600; -.
DR VEuPathDB; PlasmoDB:PKNH_0506600; -.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; B3L1G8; -.
DR OMA; TTVSCAY; -.
DR PhylomeDB; B3L1G8; -.
DR Proteomes; UP000031513; Chromosome 5.
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..377
FT /note="ATPase ASNA1 homolog"
FT /id="PRO_0000388172"
FT ACT_SITE 73
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
SQ SEQUENCE 377 AA; 42867 MW; 5BBCA47DA014D9FE CRC64;
MSDADSLSCS LTLESDEYDE EEYDTNLSKL LENKTLNWIF VGGKGGVGKT TTSCSIAVQL
AKRRESVLLL STDPAHNTSD AFNQKFTNQP TLINSFDNLY CMEIDTTYSE NTAFKLNKTE
FFDSIIPELL QSFPGIDEAL CFAELMQSIK NMKYSVIVFD TAPTGHTLRL LAFPELLKKA
LGYLISLREK LKGTLNMLKS FTNNEVELEG IYEKINHLNA MSISIQSNFQ NPLKTTFVCV
CIPEFLSVYE TERLIQELTK KNISCYNIVV NQVVFPLDCP TVNVSHCEGL LKQIKDKKIQ
ESFSSLVQKT KELEDVYISR RKLQSKYLTQ IKNLYGNDFH IVCMPQLKSE IRGLENISNF
SEMLLESKDI PIYRSEG
