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
//