ID D3KCI3_PLAFA Unreviewed; 925 AA.
AC D3KCI3;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Sarco-/endoplasmic reticulum Ca2+ ATPase {ECO:0000313|EMBL:ADC29770.1};
DE Flags: Fragment;
GN Name=atp6 {ECO:0000313|EMBL:ADC29770.1};
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:ADC29770.1};
RN [1] {ECO:0000313|EMBL:ADC29770.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=24G {ECO:0000313|EMBL:ADC29770.1}, and 9A*
RC {ECO:0000313|EMBL:ADC29774.1};
RA Jambou R., Martinelli A., Pinto J., Gribaldo S., Legrand E., Niang M.,
RA Kim N., Pharath L., Volnay B., Ekala M.T., Bouchier C., Fandeur T.,
RA Berzosa P., Benito A., Ferreira I.D., Ferreira C., Vieira P.P.,
RA das Gracas Alecrim M., Mercereau-Puijalon O., Cravo P.;
RT "Geographic structuring of the Plasmodium falciparum Sarco(endo)plasmic
RT reticulum Ca2+ ATPase (PfSERCA) gene diversity.";
RL Submitted (JAN-2010) 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; GU456711; ADC29770.1; -; Genomic_DNA.
DR EMBL; GU456715; ADC29774.1; -; Genomic_DNA.
DR AlphaFoldDB; D3KCI3; -.
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; 2.
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; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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:SF4; CALCIUM-TRANSPORTING ATPASE 1, ENDOPLASMIC RETICULUM-TYPE-RELATED; 1.
DR Pfam; PF13246; Cation_ATPase; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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 35..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..52
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 423..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADC29770.1"
FT NON_TER 925
FT /evidence="ECO:0000313|EMBL:ADC29770.1"
SQ SEQUENCE 925 AA; 104616 MW; 700A3BCF05CD9417 CRC64;
NEELDDRRLK YGLNELEVEK KKSIFELILN QFDDLLVKIL LLAAFISFVL TLLDMKHKKI
EICDFIEPLV IVLILILNAA VGVWQECNAE KSLEALKELQ PTKAKVLRDG KWEIIDSKYL
YVGDIIELSV GNKTPADARI IKIYSTSLKV EQSMLTGESC SVDKYAEKME DSYKNCEIQL
KKNILFSSTA IVCGRCIAVV INIGMKTEIG HIQHAVIESN SEDTQTPLQI KIDLFGQQLS
KIIFVICVTV WIINFKHFSD PIHGSFLYGC LYYFKISVAL AVAAIPEGLP AVITTCLALG
TRRMVKKNAI VRKLQSVETL GCTTVICSDK TGTLTTNQMT TTVFHLFRES DSLTEYQLCQ
KGDTYYFYES SNLTNDIYAG ESSFFNKLKD EGNVEALTDD GEEGSIDEAD PYSDYFSSDS
KKMKNDLNNN NNNNNNSSRS GAKRNIPLKE MKSNENTIIS RGSKILEDKI NKYCYSEYDY
NFYMCLVNCN EANIFCNDNS QIVKKFGDST ELALLHFVHN FDILPTFSKN NKMPAEYEKN
TTPVQSSNKK DKSPRGINKF FSSKNDNSHI TSTLNENDKN LKNANHSNYT TAQATTNGYE
AIGENTFEHG TSFENCFHSK LGNKINTTST HNNNNNNNNN SNSVPSECIS SWRKECKQIK
IIEFTRERKL MSVIVENKKK EIILYCKGAP ENIIKNCKYY LTKNDIRPLN ETLKNEIHNK
IQNMGKRALR TLSFAYKKLS SKDLNIKNTD DYYKLEQDLI YLGGLGIIDP PRKYVGRAIR
LCHMAGIRVF MITGDNINTA RAIAKEINIL NKNEGDDEKD NYTNNKNTQI CCYNGREFED
FSLEKQKHIL KNTPRIVFCR TEPKHKKQIV KVLKDLGETV AMTGDGVNDA PALKSADIGI
AMGINGTEVA KEASDIVLAD DNFNT
//
