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Database: UniProt
Entry: E5RU11_PLAFA
LinkDB: E5RU11_PLAFA
Original site: E5RU11_PLAFA 
ID   E5RU11_PLAFA            Unreviewed;      1228 AA.
AC   E5RU11;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=P-type calcium transporting ATPase {ECO:0000313|EMBL:BAJ53969.1};
OS   Plasmodium falciparum (malaria parasite P. falciparum).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5833 {ECO:0000313|EMBL:BAJ53969.1};
RN   [1] {ECO:0000313|EMBL:BAJ53969.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mlw619-115 {ECO:0000313|EMBL:BAJ53969.1};
RX   PubMed=20956593; DOI=10.1128/AAC.01156-10;
RA   Tanabe K., Zakeri S., Palacpac N.M.Q., Afsharpad M.,
RA   Randrianarivelojosia M., Kaneko A., Marma A.S.P., Horii T., Mita T.;
RT   "Spontaneous mutations in the Plasmodium falciparum sarcoplasmic/
RT   endoplasmic reticulum Ca2+-ATPase (PfATP6) gene among geographically
RT   widespread parasite populations unexposed to artemisinin-based combination
RT   therapies.";
RL   Antimicrob. Agents Chemother. 55:94-100(2011).
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DR   EMBL; AB576250; BAJ53969.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5RU11; -.
DR   VEuPathDB; PlasmoDB:PfGA01_010010500; -.
DR   VEuPathDB; PlasmoDB:PfKE01_010009400; -.
DR   VEuPathDB; PlasmoDB:PfSN01_010009000; -.
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; 3.
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; 2.
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; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF102; CALCIUM-TRANSPORTING ATPASE SARCOPLASMIC/ENDOPLASMIC RETICULUM TYPE; 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   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   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        64..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1046..1069
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1155..1174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1194..1212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..81
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          452..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1228 AA;  139415 MW;  810C3C8735AE5AD9 CRC64;
     MEEVIKNAHT YDVEDVLKFL DVNKDNGLKN EELDDRRLKY GLNELEVEKK KSIFELILNQ
     FDDLLVKILL LAAFISFVLT LLDMKHKKIE ICDFIEPLVI VLILILNAAV GVWQECNAEK
     SLEALKELQP TKAKVLRDGK WEIIDSKYLY VGDIIELSVG NKTPADARII KIYSTSLKVE
     QSMLTGESCS VDKYAEKMED SYKNCEIQLK KNILFSSTAI VCGRCIAVVI NIGMKTEIGH
     IQHAVIESNS EDTQTPLQIK IDLFGQQLSK IIFVICVTVW IINFKHFSDP IHGSFLYGCL
     YYFKISVALA VAAIPEGLPA VITTCLALGT RRMVKKNAIV RKLQSVETLG CTTVICSDKT
     GTLTTNQMTT TVFHLFRESD SLTEYQLCQK GDTYYFYESS NVTNDIYAGE SSFFNKLKDE
     GNVEALTDDG EEGSIDEADP YSDYFSSDSK KMKNDLNNNN NNNNNSSRSG AKRNIPLKEM
     KSNENTIISR GSKILEDKIN KYCYSEYDYN FYMCLVNCNE ANIFCNDNSQ IVKKFGDSTE
     LALLHFVHNF DILPTFSKNN KMPAEYEKKT TPVQSSNKKD KSPRGINKFF SSKNDNSHIT
     STLNENDKNL KNANHSNYTT AQATTNGYEA IGENTFEHGT SFENCFHSKL GNKINTTSTH
     NNNNNNNNNS NSVPSECISS WRNECKQIKI IEFTRERKLM SVIVENKKKE IILYCKGAPE
     NIIKNCKYYL TKNDIRPLNE TLKNEIHNKI QNMGKRALRT LSFAYKKLSS KDLNIKNTDD
     YYKLEQDLIY LGGLGIIDPP RKYVGRAIRL CHMAGIRVFM ITGDNINTAR AIAKEINILN
     KNEGDDEKDN YTNNKNTQIC CYNGREFEDF SLEKQKHILK NTPRIVFCRT EPKHKKQIVK
     VLKDLGETVA MTGDGVNDAP ALKSADIGIA MGINGTEVAK EASDIVLADD NFNTIVEAIK
     EGRCIYNNMK AFIRYLISSN IGEVASIFIT ALLGIPDSLA PVQLLWVNLV TDGLPATALG
     FNPPEHDVMK CKPRHKNDNL INGLTLLRYI IIGTYVGIAT VSIFVYWFLF YPDSDMHTLI
     NFYQLSHYNQ CKAWNNFRVN KVYDMSEDHC SYFSAGKIKA STLSLSVLVL IEMFNALNAL
     SEYNSLFEIP PWRNMYLVLA TIGSLLLHVL ILYIPPLARI FGVVPLSAYD WFLVFLWSFP
     VIILDEIIKF YAKRKLKEEQ RTKKIKID
//
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