ID V9FP20_PHYPR Unreviewed; 1602 AA.
AC V9FP20;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=F443_04298 {ECO:0000313|EMBL:ETI52523.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI52523.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI52523.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI52523.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:ETI52523.1}.
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DR EMBL; ANIZ01000779; ETI52523.1; -; Genomic_DNA.
DR EnsemblProtists; ETI52523; ETI52523; F443_04298.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR OrthoDB; 103847at2759; -.
DR Proteomes; UP000018721; 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:SF214; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000018721};
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 1178..1200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1256..1278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1298..1318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1330..1351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1371..1389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 79..133
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1142..1399
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 212..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 29..56
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 219..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..981
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1602 AA; 177759 MW; 33D6828600F125EC CRC64;
MRIQAEAVAE PRADAEDSDQ RLRVIRIDRK TLLARANAAQ RRRRREEREA RRLGNRRRSS
WLFGGAKRPR EDAVGPPSPF TGNVVVSAKY SAWNFAPRVL LAQLKRPSNV YFLFIAVLQT
IREVSNTSGI PTILLPLAVV FICSAIKEAL EDRERHRADR VTNSRPVLTL TPLGSWEQRQ
WGDLRVGDIV KVMNDQTVPA DLFLLSAEAV EHDDDGPRPQ QLQVTNSQGS TDLEKGKDSA
IDRSELLLDI QGDQGPVSPK QQSAESNLAY IETKSLDGET NLKIRTAIPL VASLCRGSST
KSRTIEGGGY NELRGMMVCE QPNNRITSFD GTFSAILSPA QAEMLGVAAN DPNSAQLAAP
VQTASLLQTE MTGDGLVRVR VPVTAKQMML RSCVLRNTRS VTGMVVFTGH ETKVFCSNTE
PVVKTSSVER RLNRLIIGIV FIQQLVCFLG ALLGAHWMHT EGDSFWYLLS ASERRHHNLT
GASTSHPLAE LAKLHLRYFI IMQNFVPISL NVSLEFVKYW QAYFIEQDLE MYDKPSDTPA
MVRSSALNED LGRVHHIFTD KTGTLTMNLM LFRYCMVGGK HYGGLMQDKD MEAEMSNETL
STAGDSQDGP RFVDFDPTEL FADIHAGGEQ AETLRRFLRH LALCHTLIPT KSLTEMCSTS
FPEYSASSPD EQALVSAAAF CNVRFVHRTP TAVMLLEPGW TSPSSYKLLN VLEFDSDRKR
MTVIVETPDG AIELLCKGAD NVIFERLGAD QAAMPGRMSS EQASEQLTLY AKAGMRTLCL
AYKTISRQEY ENWNARYTQA HASMEELVKR RQGRANAIDP LMNEIERDLV LLGVTAVQDK
LQAGVPATLR LLQETNIKVW TLTGDKMETA VNIGYASALL SHDMDVQQIG GDGYTSTAAA
LKELSQRGDQ EATSYHPSPF LASLSSRTNG GRGMRRSRRR ASIQTDNFLG SAKAAISEFL
FGPPTKQKRK QKRRRPRNRR TSRTSSAFSQ TPMYSSVATD AEYVDRFTSD EESLYDVGIE
ADDEAVHTPE YGSLAGNLDS REGRQSGSNS QKLALVIDGQ ALEYALRPQL RSLFYQVTQQ
CASAVICCRV SPKQKADIVE FVREFEPDSV TLAIGDGAND VAMIQSAHIG VGISGQEGAQ
AVNASDYALA QFRFLQRLLF VHGRWAYRRV AKLMSYMLYK NVTYVLTTFW FGCFCGFSGQ
PLILDVAAQS FNVLYTSVPL VLFAVFDQDV SSTSAAKFPY LYALGQKNIL LARRVFWPWI
FNGVWHSIVI FFVSAWAFEG FGLSIRDFPV IATETGKSGG LVTLGFVVFT NLVIVVNLKL
CLETFMLTWQ FLLTVTVSIL LWFAVGSLIS LPNTGFPQAT GEMEYLQELP TFWLVCLLVL
SLSLLRDGLW KIVRRFSLPS MYHILQEREV MGLPNSPRGM LREHRRSVSN TAWSDEPATV
VDYAKLFTRL ESPEETLMRS SPLGERLIAS PFSSSSSGGD TIDPDHMAGF QGREKKRNIR
IRGSFHSIDS FDSFDAGVEP SFLEAPGSVA ATSTVNAAIG SRTSSFVGSY HGYAFSEDEN
VDSDVEAASS RTSRGDVDQT KIALSHASIK KVLKSVRGRK NA
//
