ID A0A078B4W6_STYLE Unreviewed; 1073 AA.
AC A0A078B4W6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=Contig17066.g18182 {ECO:0000313|EMBL:CDW89464.1};
GN ORFNames=STYLEM_18597 {ECO:0000313|EMBL:CDW89464.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW89464.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW89464.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW89464.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) 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; CCKQ01017571; CDW89464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078B4W6; -.
DR EnsemblProtists; CDW89464; CDW89464; STYLEM_18597.
DR InParanoid; A0A078B4W6; -.
DR OMA; QPYVWLT; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000039865; 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; 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; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000039865};
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 43..60
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 808..826
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 838..857
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 877..898
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 16..67
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 701..818
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1073 AA; 122956 MW; 1371D10FD16CAF80 CRC64;
MFGKNEQALP LHQIKKSNSI RTTKYTILSW APLSILFQFK RAANIYFLII SVLTCLSFSP
KSPISMIGTF AAVLIFTMFK EAYEVLERKT NNFKEKKWSN VKIGDILLVN KDMEFPADLL
LLNSQKDIVY VDTMNLDGET NLKEKYVFNQ DFNLVQISDF EGYVCCDIPN ENLDEWDGNI
VLGKDQIINC RTGDENHEKC QETSKKGFQH YEENELNALH CFWLLTFWVA YSHLIPISLY
VIIEMLKLTQ AYLIGKDLKM YDIETEQFGI CRNSDLIEEL GQVDFIFSDK TGTLTQNKMI
FKKCSVGNVI YGESQQIDDP QQDELVQSSK EKILKEMFDN KQFSEHGQQL MQFFRTLAVC
HTCMVERDKD SGKLKYSSSS PDELALVQGS KQVKIEYIER SSTNIKIKLN EDETEEYELL
VEFPFDSTRK RMTLIVRNSQ TKMITQMTKG ADSIMIPRIN FGKNEQAQVE KDLYKFACEG
LRTLVFGSKI LSQDDYLEFK KQYDNLKIST DSKKDEKLNI LFDEMEYGLN YLGSSAIEDK
LQEGVADTID TLINANIRVW VLTGDKQETA IEIGKSCKLI QSNMKEVVLT SKNRDDFKTR
LKGYSSQEYK QKLAIIIDGP TLIYALEDSL TAQQFFAFGM RANSVICCRV SPKQKADVVA
LAKKQKKFIT LSIGDGANDV SMILEAHIGV GIRGKEGTQA VRSADYAISQ FRFLERILLV
HGRYGYMRVS NMICYYFYKN VVLVFTELHF AYWNGFSGQI FFADWLPTLY NAFFTSWLCL
FALMLERDVD DESSQRSPQL YAAGQKGHYF NFKVFLLSLS LLLDLLEVDS VKYFSRCIAA
FISLAIYYGA LFLLSYYKLS QLIQNELTGT FLQLFQPYQS IYCLIVLPFA LLIPDGLIKL
TQKIFFPSPS DALMINILEE IDNNGQKSTE QVKNLLSDNA MDNEIKNQLN TSSQNNSFIN
VSPTHKLLDK NSSNEQNKAN ISKIIQPSRQ QPLNLSSLNG SIQLDMGIKN KLINKLDPSA
NKFAQQNEKN KAIEKKNNDQ SFLLPQIKQQ LVINNSATYH YSDSISQPNE INY
//
