ID A0A024VQD4_PLAFA Unreviewed; 1264 AA.
AC A0A024VQD4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Potassium/sodium efflux P-type ATPase, fungal-type {ECO:0000313|EMBL:ETW30121.1};
GN ORFNames=PFFCH_02432 {ECO:0000313|EMBL:ETW30121.1};
OS Plasmodium falciparum FCH/4.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1036724 {ECO:0000313|EMBL:ETW30121.1, ECO:0000313|Proteomes:UP000030656};
RN [1] {ECO:0000313|EMBL:ETW30121.1, ECO:0000313|Proteomes:UP000030656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCH/4 {ECO:0000313|EMBL:ETW30121.1,
RC ECO:0000313|Proteomes:UP000030656};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum FCH/4.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW30121.1, ECO:0000313|Proteomes:UP000030656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCH/4 {ECO:0000313|EMBL:ETW30121.1,
RC ECO:0000313|Proteomes:UP000030656};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum FCH/4.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KI927935; ETW30121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024VQD4; -.
DR EnsemblProtists; ETW30121; ETW30121; PFFCH_02432.
DR Proteomes; UP000030656; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF128; CATION_ATPASE_N DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030656};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 165..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..944
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 996..1023
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1201..1223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1229..1250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 118..193
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1264 AA; 140361 MW; C28E1755E1433C4A CRC64;
MSSQNNNKQG GQDINNKKDS DDIKPSVSKE DLINSLKNDE LNKNTTMDQN DMKKNENMNI
KKNEVLNNSN NVEDGDNENS KFMNKSKEGL NNINGEKNDD NNSIVKVEES PKSIGYNYYA
SESIENLCKE FGLESINTGL NSEQVKINRD KYGENFIEKD EVVPVWLIFL SQYCSPVVLL
LLVAAVASLA LNEVVEGVAI ISIVTLNACL ATYMEKSSGD AIGKLAEMAS PQCTVLRNGQ
KVVIPSREVV VGDVVLINTG DSISADLRLF DVIELKTNES LLTGESEDIK KTIVADNLST
PFATNLCFAT TSVTSGSGKG IVISTGLDTQ VGKIASQLKK SSKGSKLTPL QVALNKLGGL
IGLIAIIVLV VIISLAVIIK YRDPAHADKD PTFVIIIIGV GFAVSSIPEG LPMVVTITLS
AGAKDMVKKN ANVRKLPAVE TLGCCSVICS DKTGTLTEGK MTAINAVTIC KNSSLSDENN
KLTKTFDFYP TKGFEPCGGL FDSNELTSEK KKEIVIAKNQ NTSYDKVLYN YGNPSNKSVI
VDKTRSLMFA AYLNSYDTTL SRDPKTLKWG IHGNMSEGPI VVAAAKVGYS FINNPNHKSY
LDNFQRLDDL EVTFNSSRKM KITFYKLKTV NVFENVYLDK PGKVYTHVAL IKGAPDRLLD
RSTHLLEETS MKKVQVSWNS TITQEERNVL IKKNLELSQK ALRVLSICIK PLTDQNIEEL
KKLEDADERL KYVNYDENGG FIPMGYVASF DPPRPGVKEA IQTCREAQVK VIMITGDQKP
TAVAIGKLIG LIEEKSEQVE DINSLAIECS ELHINKNPNE PILPNDQLDE FTDKILIYSR
AQPEDKITIV QSLKRKGYLV AMTGDGVNDA PALKAADIGV AMGINGTEVA KGASEMILID
DNFCTVVSAI DVGRTIFSNI QKFVCFLLGT NIGEIIYLSV AIVAQMPFPL EALQILFLNL
MTDGCPAVAL SREPPNDDNM KTPPRPKKQP IMTKRWWFYG ILPHTIFEAL CVLLSLAFSL
YICTGFYNLN GIHNLCKTVN LVDVNDANVY HEYKYFCSSY EYRISTDYVG WVTNVSFWDP
KNNEAVNFWG AAKGKVENIN PLSDIVHPEL RLRMQDGCSG DLTLDENRWC RPKDNKTSDG
YNDELEGILK KGFEDVTAKG SKRGRTMAFI SAVWCEMLRA YTVRSWEPFY KVFNRNMWMH
LACSISATLT FLSTCIPGIT SILNTTCLLW WQYLLAIFWA LLNLFLDEIV PKVIYRRKYM
TIKN
//
