ID D0NRR5_PHYIT Unreviewed; 1391 AA.
AC D0NRR5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=PITG_15139 {ECO:0000313|EMBL:EEY63415.1};
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY63415.1, ECO:0000313|Proteomes:UP000006643};
RN [1] {ECO:0000313|Proteomes:UP000006643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
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; DS028155; EEY63415.1; -; Genomic_DNA.
DR RefSeq; XP_002898300.1; XM_002898254.1.
DR EnsemblProtists; PITG_15139T0; PITG_15139T0; PITG_15139.
DR GeneID; 9476020; -.
DR KEGG; pif:PITG_15139; -.
DR VEuPathDB; FungiDB:PITG_15139; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; D0NRR5; -.
DR OMA; DMMIYQR; -.
DR OrthoDB; 103847at2759; -.
DR Proteomes; UP000006643; Partially assembled 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 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:UP000006643};
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 390..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 434..459
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 987..1005
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1025..1042
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1063..1087
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1107..1125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1137..1158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1178..1197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 116..181
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 956..1207
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 27..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1391 AA; 153601 MW; BA43471938E96069 CRC64;
MAAKRSTSRI FRGSRVEDQV ALCSSVAPAR DDSALSDQSD NALGSSTSGY NTLGSPALLQ
SPRQIRRKSK QTKEQLLDED ELVDYAAQHT PASTSGSGQP GAAAGAPGPD ETLREVYFNY
APGNAVFDKC SNVVVTSKYN VATFLPKFLK ESFSKVANFF FLMVCVLQSI PSISNTYGYP
TNAPVLFFVI SIDAVFAVME DLRRHQSDNE ANSATCHVIQ DGQVVDKKWA DIKVGDFLQI
RNREVIPADV LVLAVAEPVG EPPSGICYVE TKSLDGETNL KLRQAVAATM SSLSNAAELA
LLRGVIKCEQ PNPHINKFAG KVEVTVGDGC GVEVMPLSVK NVLLRGCNLR NTDWVFCLVL
NTGNDTKIMQ SASAAPSKWS DLMLNINRMI VILCLGLFVA CAMAATCYIT WQYDIVRNAW
YIQLSESERN RTRLVAFIQM LFYYFLLLYQ VIPISLYVSM TSVKFLQSRF MSWDLEMYHA
ETDTPAIVRT MELNEELGQI SYVFSDKTGT LTCNVMEFRK CSINGTSYGS GITEIGRAAL
VRAGKPIPPE PKLDPSVKSI PFVNFVDKSL FDSMKGSAGE EQKEKIMQFF EHLAVCHTVI
PEKLESGEVR LSASSPDEQA LVAGAAFAGF KFESRRVGTA LVDVLGQRVT YEVLDVLEFN
STRKRMSVVV RKPSGELLLY TKGADMMIYQ RLKDDPAMLK LKNITRDHME KYADDGLRTL
ALAVKKLDER WFQQWKMRFD DAQGNVAEID RRKDGKPNAI DALMEEIEEG LELIGATAIE
DKLQDGVPQC LANLTRAGIK VWMLTGDKEE TAINISYACS LLDNSIQQVI VNATTCPDEA
AIRAKLNAAA REFLDGAKGM AGGSEKEISL VIDGEALEMA LRPGTAPHLL SFAKLCRAVI
CNRVSPAQKA EMVKLVRDNI TTVRTLAIGD GANDVAMIQA AHVGVGISGQ EGMQAVNSSD
YAIAQFRFLE RLLLVHGRWN YIRISKLVLY MFYKNITLVL AQYWYGYLSG ASGSKMYWEI
GVQLYNVAFT GLPIVVVGVL DKDLPAPFSI EYPDLYRRGP DRFFFNMYTF CRWIAAAFYE
SLIIFVVMSY GFNASEKSAG SESRVEFGMV AFSLTVLIVN IKIWMIADRW TLLSFSLWFG
SVMSWFGFAA IGTETPYFAT FKIGYDEFGA FAPTAKTWGY FLVLIMGCSL ALGRHVAYNL
YQRTFHPDLA QLLQESMGGG SQRKYQRRLT INHMEEQTLS MSLDDVHTTG YLSDFGHSDA
EILKAQHPQS FAATLYEQQP KKSASNVGTS APQSTSSGVT DSYSASVFSE SISEDATWER
VPTKMFRGTT GRRNTGFAFS CDEETTLAES YIASNSLPRS DAISTAMRNS TSSTGGASAG
RVSMGRVRLL S
//
