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Database: UniProt
Entry: A0A1J4KBC0_9EUKA
LinkDB: A0A1J4KBC0_9EUKA
Original site: A0A1J4KBC0_9EUKA 
ID   A0A1J4KBC0_9EUKA        Unreviewed;      1141 AA.
AC   A0A1J4KBC0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=TRFO_04795 {ECO:0000313|EMBL:OHT08713.1};
OS   Tritrichomonas foetus.
OC   Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC   Tritrichomonas.
OX   NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHT08713.1, ECO:0000313|Proteomes:UP000179807};
RN   [1] {ECO:0000313|Proteomes:UP000179807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA   Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA   Tasca T., Bogo M.R., de Souza W.;
RL   Submitted (OCT-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OHT08713.1}.
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DR   EMBL; MLAK01000660; OHT08713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4KBC0; -.
DR   VEuPathDB; TrichDB:TRFO_04795; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000179807; 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   CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
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; 1.
DR   PANTHER; PTHR24092:SF150; 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; 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   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:UP000179807};
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        52..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        76..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        268..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        313..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        842..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        917..938
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        950..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        980..1000
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1020..1040
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          19..76
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          802..1047
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1141 AA;  127700 MW;  28435790E681107A CRC64;
     MSGAEEKGRS VVIHMTRNAK GKKLFMDNGI STTKYNVLTF LPKNLFEQFS RIANFYFLVT
     ACLMFFPWSP LESTTALLPL AIVVLISMVR EGIEDFMRYL SDRKVNATKV DHLDGNTFKD
     IEWRKVLVGD VLLIKKNEQI PADVVLLNTS EPEGIAYVDT CNLDGETNLK VRQALPQTKS
     VVDAVTAAQF QSTIVCDSPN NFLYTFNGYM TIVEKNCSLT NDQVILRGCV LRNTAWAIGV
     VVYTGLETKL MMNSSAARSK RSSLERGLNL KLISVFAFMI VLGIISASIG VAREKDLVNT
     GKSWYLYQGK TRSAASAFFI LMFSYILLMN AMIPISLYVT LEVVRVFQAL FIAWDKGMYH
     IETKTSASAR TSNLSEDLGQ IDYVFSDKTG TLTRNVMEFM KCSIGGEKYG KGITEVAYAA
     AKRRGIACQP PDNVGKAFKD ERFMQLLKKD TPPIVRHFMW MLSVCHSVIP EEDSTKPYGI
     AFQASSPDEG ALVGAAADFD YIFKQRGPGY VVVGHKGEDV RIEVLQTIEF TSDRKRSSVI
     LRSPDTGEIV MYTKGADDCI MERLAEGAEF RAITMQHLRD FAADGLRTLC CAYKIIDEGF
     YNSWAARFNE ANCLIEGREQ AVAEIADEIE RDLHLLGATA IEDKLQIGVP DAIEAILQAG
     INVWIITGDK RETAINIGFA CSLLASDMTL IVLDSSDPAE IQRTIHQGLG RPGKLALIAS
     GAALYYAMDE DNKDTFFALT ERCQSVICCR VSPLQKAKIV ELVRKKTGKL TLAIGDGAND
     VGMILKADIG VGISGQEGRQ AVMASDYAFG QFRFLKRLLV YHGRLNLMRN VELINYSFYK
     NMVYTLNQFI FGFFCNFSAM TLFDGFLYSI FNVVFTSCPP VVYAGMERDI SERRLMAFPE
     LYKWDGNRKW MISYGNFWLS LSIGILHCLI SFLVPYFGMA PYVDGNGQSI GYGGFGITVY
     GCVVAIVTTR IAMMTTYWTW IAHVFIWGSA CLYPLAVLIL DYSGLGKEIQ GLSVPTLGSI
     QFWISIIGSV VLANLPVIAF KTVMNSLNLM TNKVMLIERT KVKAKEARRQ FELKNIETEE
     QQIIGRYVDE KNETGYNFDP PVSMYRIQRF EQPSETTYYT ADAIRERIRP RMVSTFGLDQ
     L
//
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