ID A0A0W8D8K2_PHYNI Unreviewed; 1391 AA.
AC A0A0W8D8K2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=AM587_10003580 {ECO:0000313|EMBL:KUF92685.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF92685.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF92685.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) 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:KUF92685.1}.
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DR EMBL; LNFO01001315; KUF92685.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8D8K2; -.
DR EnsemblProtists; KUF92685; KUF92685; AM587_10003580.
DR OMA; DMMIYQR; -.
DR Proteomes; UP000052943; 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:SF214; 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:UP000052943};
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 155..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 389..410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 440..459
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 986..1004
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1024..1041
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1062..1086
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1106..1124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1136..1157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1177..1196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 115..180
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 955..1206
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 27..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1391 AA; 153986 MW; 983A2D4B4E9F691F CRC64;
MAAKRSTSRI FRGSRVEDQV ALCSSVAPAR DDPALSDQSD NVLGSSTSGY NTLGSPALLQ
SPRQTRRTSQ QTKEQLLDED ELVDYASQST PASSGSGAPG AATAAPGPEE TLREVYFNYA
PGNAVFDKCS NVVVTSKYNL ATFFPKFLKE SFTKVANFFF LMVCVLQSIP SISNTYGYPT
NAPVLFFVIS IDAVFAVMED LRRHKSDNEA NSAICHVIQD GQVVDRKWAD IKVGDFLQIR
NREVIPADVL VLAVSEPVGE PPSGICYVET KSLDGETNLK LRQAVAATMS SLANAAELAL
LRGVVKCEQP NPHINKFAGK VEVTVGDGCG VEVMPLSVKN VLLRGCNLRN TDWVFGLVLN
TGNDTKIMQS ASAAPSKWSD LMLNINRMIV ILCLGLFVAC AMAATCYITW QYDIVRNAWY
IQLTETERNR TRLVAFIQML FYYFLLLYQV IPISLYVSMT SVKFLQSRFM SWDLEMYHAE
TDTPAIVRTM ELNEELGQIS YIFSDKTGTL TCNIMEFRKC SINGISYGSG ITEIGRAALV
RAGKPIPPEP KLDPSIKKIP FVNFVDKSLF DSMKGSAGEE QKEKIMQFFE HLAVCHTVIP
EKLESGEVRL SASSPDEQAL VAGAAFAGFK FESRSVGTAM VEVLGQRVTY EVLDVLEFNS
TRKRMSVVVR KPSGELLLYT KGADMMIYQR LKDDPAMLKL KNITRDHMEK YADDGLRTLA
LAVKKLDERW FQQWKMRFDD VQGNVAEIDR RKDGKPNAID DLMEEIEEGL ELIGATAIED
KLQDGVPQCL ANLTRAGIKV WMLTGDKEET AINISYACSL LDNSIQQVIV NATTCPDEAA
IRAKLNAAAR EFLDSAKGMA GGSEKEISLI IDGEALEMAL RPGTAPHLLS FAKLCRAVIC
NRVSPAQKAE MVKLVRDNIT TVRTLAIGDG ANDVAMIQAA HVGVGISGQE GMQAVNSSDY
AIAQCRFLER LLLVHGRWNY IRISKLVLYM FYKNITLVLA QYWYGYLSGA SGSKMYWEIG
VQLYNIAFTG LPIVVVGVLD KDLPAPFSIE YPDLYRRGPE RFFFNMYTFC RWIAAAFYES
LIIFVVMSYG FNASEKGAGS ESRVEFGMVA FSLTVLIVNI KIWMIADRWT VLSFSLWFGS
VMSWFAFAAI GTETPYFATF KIGYDEFGAF APTAKTWGYF LVLIMGCSLA LGRHIAYNLY
QRTFHPDLAQ LLQESMGGGS QRKYQRRLTI NHMEEQTLSM SLDDVHTTGY LSDFGHSDAE
ILKAQHPQSF AATLYEQQPK KSGSNVGTST LQSTNSNVTD SYSASVFSES ISEDATWERV
PPKMLRATTG RRNTGFAFSC DEETTLAESY IASNSLPRSD AISTAMRNSS TSSTGGTSAR
RVSMGRVRLL S
//
