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Database: UniProt
Entry: A0A0A1U6Z5_ENTIV
LinkDB: A0A0A1U6Z5_ENTIV
Original site: A0A0A1U6Z5_ENTIV 
ID   A0A0A1U6Z5_ENTIV        Unreviewed;      1080 AA.
AC   A0A0A1U6Z5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=EIN_405090 {ECO:0000313|EMBL:ELP90095.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP90095.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP90095.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP90095.1,
RC   ECO:0000313|Proteomes:UP000014680};
RA   Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC         phospholipidSide 2.; EC=7.6.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00034036,
CC         ECO:0000256|RuleBase:RU362033};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC       ECO:0000256|RuleBase:RU362033}.
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DR   EMBL; KB206537; ELP90095.1; -; Genomic_DNA.
DR   RefSeq; XP_004256866.1; XM_004256818.1.
DR   AlphaFoldDB; A0A0A1U6Z5; -.
DR   EnsemblProtists; ELP90095; ELP90095; EIN_405090.
DR   GeneID; 14889129; -.
DR   KEGG; eiv:EIN_405090; -.
DR   VEuPathDB; AmoebaDB:EIN_405090; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000014680; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015914; P:phospholipid transport; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006539; P-type_ATPase_IV.
DR   InterPro; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR24092:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362033};
KW   Hydrolase {ECO:0000313|EMBL:ELP90095.1};
KW   Magnesium {ECO:0000256|RuleBase:RU362033};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014680};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362033};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM        111..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        310..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        334..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        822..844
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        850..874
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        904..926
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        932..951
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        958..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        990..1013
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          56..113
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          792..1018
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1080 AA;  123688 MW;  B0DB2F2F7C8378A8 CRC64;
     MEKTDLSTDI PLVSSSDDDW LFPVDKRKWY EKIPFTHWYK KFYMPRTIKR TTVEIKKAPK
     YVTNKIANTR YTWWNFLPMS LFNQFKYFYN LYFLLNASSQ LIPAFKVGMT FTYFAPLVFV
     VALSICKDAV DEIRIKLRDI KLNNEEFEMV SQGQFIPVKS KDIKVGQLLR LKKGQRVPAD
     LVILQSADDE GTCFIKTDQL DGETDWKFRK CIKEFQGLPI AELETSEFDL DTEAPHNAIY
     SFIARVRKGY DTIPVSIDNT AWANTILVSE EIVGIVIYTG KETRSSMNRN DQRNVKVGRV
     DMALNRVSKV LFCIMLALSL LMVCPDVFHG IFSFFTVVTV VRFMVLYSSI IPISIRVNLD
     ISKLIYSFFI STDDKMEGAE VRNSSIPEEL GQVQFLLSDK TGTLTKNEMS FKVLSLGTQS
     YSVDSAEEMK DELKEYLQTD NTQRVMKNSS TSKMAECIKA LALCHNVTPC VTASGERYYQ
     ASSPDEVALV KFTEQVGVIL KEKTFAKMVL DVEGREERFE ILNMFPFSSS TKRMGVIVKS
     DEGIVLYMKG ADSIMAQLID NIEWLGEECG NLAKDGLRTL VFGKKIIPSD VYEVFKKEYN
     VASSMMIGRE EAVAKSVSKI EGHLHMLCIT GVEDELQDDV QQSLEMLKRA GIRTWMLTGD
     KVETALCIAK STRLVSVDQE VREFFASSSL EAEALMEKYG GNINEEGLIV DGSTLSLVLK
     ELPMRFIHFA LQAKSVICCR CMPTQKAEVV NLVKKSGIRT CAIGDGGNDV SMIQAADVGL
     GIEGKEGKQA SMAADFSMKQ FSHVTRILLW HGRNSYIRSS DLALFIMHRG MIISIMQAIF
     SAIFNFAPVA LFQGFLLMGY ATYYTMFPVL AIVLDERVNE QKVMEFPELY YQLQTKQRLS
     MTSMLTWVSV SILQAVVIMF LCMFLFKETF LDIVSISFTA LILIELINVG FSIKRWNWLI
     LSSELFSVTI YFLSFFFLKS YFDLHFVFSW QFWWKLFVIV VLTSIPFIAK FIYQIIFPPK
     SLTVENRRWP VSFNTKCPKM PKIKMFKKYN KYFKWFNPLN WCACKKKNNQ GPYEQQMVDL
//
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