ID A0A5B8MRD2_9CHLO Unreviewed; 1281 AA.
AC A0A5B8MRD2;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=A3770_09p55210 {ECO:0000313|EMBL:QDZ23003.1};
OS Chloropicon primus.
OC Eukaryota; Viridiplantae; Chlorophyta; Chloropicophyceae; Chloropicales;
OC Chloropicaceae; Chloropicon.
OX NCBI_TaxID=1764295 {ECO:0000313|EMBL:QDZ23003.1, ECO:0000313|Proteomes:UP000316726};
RN [1] {ECO:0000313|EMBL:QDZ23003.1, ECO:0000313|Proteomes:UP000316726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1205 {ECO:0000313|EMBL:QDZ23003.1,
RC ECO:0000313|Proteomes:UP000316726};
RA Pombert J.-F., Otis C., Turmel M., Lemieux C.;
RT "The complete nuclear genome of the prasinophyte Chloropicon primus
RT (CCMP1205).";
RL Submitted (JUL-2018) 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; CP031042; QDZ23003.1; -; Genomic_DNA.
DR STRING; 1764295.A0A5B8MRD2; -.
DR Proteomes; UP000316726; Chromosome 9.
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 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:UP000316726};
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 352..374
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 402..426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 954..972
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 987..1007
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1042..1063
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1075..1098
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1107..1126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1146..1166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 44..104
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 923..1175
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 238..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1281 AA; 143075 MW; 91C07B531ED0A6E5 CRC64;
MGAERRRAGS SQLKPGQMSA LLSQTSGAAG NVSSEEVRTV FTNSSDHLWR KQMRNNRTRT
AKYTIITFFP RSLYEQFRRV ANVYFTLVAG LSLTDVSPVR PWTTFTPLAI VLGVSLVKEA
IEDYKRHQAD KKENGRQVDV WCKDKVGWKT VRWDQVKVGD VVRVTRDQGF PADIVLLSSG
TSDGVCYVET MNLDGETNLK LKKAIGATNG MDTSNFDGFN TAVQCDLPNP SLYTFTGNIH
LLGQPPQRRG SEDQSARSRA GSASSVGSRG RSGSGASVEG SEQLPRTRSK VNYEIKTYPV
SPESILLRGS NLRNTEVVYG VVVYTGHESK VMMNATEPPS KRSSLEKSID SVIMFQFTLL
FFMCVSGSVL SGFWHEYYGY QHWYLALDDK PKEFTPEDKI KVMGLSFITS FILYGYLIPI
SLYVCVEMVK IVQAMIYIRC DREMYHEETD TAALARTSNL NEELGMIDTV LTDKTGTLTC
NVMEFFKCSI NGKTYGTGVN EIEKANSLRK GLTIDQIMEG SNQRTSEPVK GFSFYDEEVS
DFAWTGHKDV KEIQMFLQLL AVCHTVVPEG EADDINYQAE SPDEEALVLA AKEMGYKCVK
RNLNSLFVQE RDLGGEIKEK EYKILHVLEF TSARKRQSVI FKTPEGEIIL GCKGADNVIY
DRLAERTGEV QENTQDHLNA YAQAGLRTLC ISYRKLSDEV YSEFHKKWTE AKTALSDRDV
KVEAVNDKIE RELILVGATA IEDRLQDKVP QCLELLANAG LRIWMLTGDK LETAVNIGYA
CSLLTDSMSV HTVQLNLGDT RLSVDSTHEE RSKVFTLQVT EQFAKISKRV MKGTDLHALV
IEGNALAYAI TPENADSLID ICGSCASVIC CRVSPRQKAQ VTELVKLSGA TTLAIGDGAN
DVGMIQAAHI GVGISGKEGM QAVMSSDFAI AQFKFLERLV LLHGRISYKR LGRMVGYFFY
KNIVLGLCLY FYNSQAFFSG QTLFDDFYLS CYNILFTSLP VLAVGVFDED VKYKTVRKYP
RVYEQGALRN EYFSFFPVRT MWVLNAVYAA IVNFLFVLCS YGMDADKENG KVSGLFSMGT
CLYTTIVITV NIQIALVLDH WTIFHHFAIW GSILCWFLFL IVYGSFDPDI SQNVYQLFLT
IVVPTTRYWL IIVIVPLVAV LPDFFVRQLK HFKFPSDHRV LQEVEVYHLR GDMDRQQNVD
LRNSRLSSLT LPSKGASKIR IKSLMSRRVS EVPQATAAAP SSSVASSSSQ ESLVVVQNPA
ALPGASEIIE KVVTPVGGGS H
//
