ID A0A0W8AY92_PHYNI Unreviewed; 1597 AA.
AC A0A0W8AY92;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=AM587_10016890 {ECO:0000313|EMBL:KUF64626.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF64626.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF64626.1, 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:KUF64626.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNFO01006124; KUF64626.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8AY92; -.
DR EnsemblProtists; KUF64626; KUF64626; AM587_10016890.
DR OMA; GWFLWNI; -.
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 NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF218; P-TYPE PHOSPHOLIPID TRANSPORTER; 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 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|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 126..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 164..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 202..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 349..365
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 587..610
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 630..651
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1271..1289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1301..1324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1354..1384
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1404..1425
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1437..1456
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1476..1495
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 315..373
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1240..1504
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1086
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1597 AA; 178721 MW; AFD1FEEC07431FB3 CRC64;
MRVEFAVPSP SDSATDYTLD MGTQTQPPAS ADRAAPAPSA PKNLRRVNTF TGAVNEEEAR
NIISLRYRAD SMADSVASDS KPNAETKLWN LFEQVFCFLK GMTIYQTRRR LKFTIVSQTV
INSLRIFPII LGLSFQATLP VLILYVTLVL GWHGTKFLVP KFLLSYKIGM QLTLLVDVIW
YYKGYNGKLN SVSSGTSVLM QGFFSILLTM LNITGFMYGW KLRRIVKAVQ NQRECDRAAL
ATMMPSPQRV NSLHQTLSIN PSAEMDEEEV PSARRKITVG PGVPNNRTRR TQSGVPASLP
DVLKTKKQRR KEAEAQEEAP VFCSNLIITS KYTYYNFLFV FLKMQFSRLA NLYTTIVVAL
CFFDFSPVSP VASLTPLLIV FATSALKDVS EDRRRQKGDA QVNSRSAHIV RRDVLDEVMH
IDGTWQDIEV GDVLLLKDGD QVPADCILLA TSRPDGRCYV ETANLDGETN LKIRQVASCT
KHFLTAEEIL DRYTLEVECD VPNKDLFYFD GVLKLKKFAD EAVADTTNKE DTETSLTMDN
LILRGSESRN AEWTLGLVIY TGKETKVQMN SVAVPLKRSF VEKTLDTMFV LVLMLLFGIS
IACTLGNNNW NLDLADDSTP WYIKEDSNGY IFLSYVILFN NLIPLSMYVT MEGVRFVHAR
YIENDLEMYD VKTDTPAQVR NSNINEDLGQ IQYIFSDKTG TLTCNEMIFA KCTIAGLRYN
DIEVDPAKRA RPGTRFNDGR LLARLNSNHS TKKEIHDFLL LLTICNTVIP ETNVPTSPTS
SSDSCSVETP TIKYNASSPD EEALVLAAAD LGYVLESRDG SLCHTLIQGR PMSFEILNVL
EFNSDRKRMS VIVRFPDGSI VLYCKGADDI IFDLLSKSQP QGVAHVTRGH LQEYASEGLR
TLTTAMRRLT QEEYDQWNQL YRQAEFSMEG RAAKIAKVSA IIEVELTLLG ATAIEDRLQD
GVEESICALR KAGIKFWVLT GDKKETALSI GMSSHVIDDN MDVIVLGQRD KGSLRARLEE
LYVDLVEDKW GSDETSSATS VLLEALKRAI LYLWDLVKLA LVGRDEEAEA RKKRRRLPRR
EHAGADAAPT DSPAHYDEVY PALPNRDITE NSFNRDLCDH DFEPKTDNMT GGTNSMSSGD
FIDEELEFAM VIDGKTLALV LDDDIKYLFL AVATQCKSVI CCRCSPSQKA SVVKLVTEPT
LMFSPGNITL AIGDGANDVP MIQAANVGVG ISGKEGRQAV LSSDYSIAEF QYLKRLLLVH
GNYSYKRISK LILFSFMKNV ALSMSNFFLA METMYSGLLM YFSIFFTLYN ALFTTIPIVV
IAMYNQDVSP AVLMQYPTLY VNGLKNRSFN WLSFFGWCVL GAWHAYVVYA VPFFTNGSIV
WYFSSDSSKL QFDKRDLGLW ANGVASYTYL ITASTVQVSL MTSNWTRANV LSTVGTLVFY
YLFTAFFCAV FGWTKADFYD TEVGYGVVSQ LVNEGWFWLG LLFSVVVAIL PNYIAKAGRV
LFYPEPSHLM REWNRLAKGE DAAVVMDSPR LVRRNTGFAF SHCPGESEMA LGVYRSSNMR
EQSRAGQRSD LSNVGMRVQS PSSSTADGSS PSPKALD
//
