ID A0A0B1P0G0_UNCNE Unreviewed; 1507 AA.
AC A0A0B1P0G0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=EV44_g5396 {ECO:0000313|EMBL:KHJ32142.1};
OS Uncinula necator (Grape powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ32142.1, ECO:0000313|Proteomes:UP000030854};
RN [1] {ECO:0000313|EMBL:KHJ32142.1, ECO:0000313|Proteomes:UP000030854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX PubMed=25487071;
RA Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA Walker M.A., Cantu D.;
RT "Adaptive genomic structural variation in the grape powdery mildew
RT pathogen, Erysiphe necator.";
RL BMC Genomics 15:1081-1081(2014).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
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:KHJ32142.1}.
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DR EMBL; JNVN01002298; KHJ32142.1; -; Genomic_DNA.
DR STRING; 52586.A0A0B1P0G0; -.
DR HOGENOM; CLU_000846_0_1_1; -.
DR OMA; QALRCGR; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000030854; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
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; IPR008004; OCTOPUS-like.
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; PF05340; DUF740; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
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:UP000030854};
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 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 171..187
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 514..539
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 559..582
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1130..1149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1161..1182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1212..1233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1253..1271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1278..1300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1320..1338
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 116..166
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1098..1347
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1507 AA; 171201 MW; 9CC73DAEAE21C4B1 CRC64;
MVLSNYSGSE DTPKSVQKLK WVNQRLKDQN RGSRKRKLVS KRTTQRRSPN NEKGKDISNP
DSVNADQGHT QEQLAAGRES EDATKGYDQL DQAPRNIYFN IPLPPEALDE DGDPLVQFKR
NKIRTAKYTP LSFVPKNIWF QFHNIANVYF LFLIILAFFS IFGASNPGLN AVPLIVIVFI
TAVKDAVEDY RRTVLDNKLN NSPVHRLIDW NNVNVNEDDV SNWRKIKKAT SHTLLGLWSQ
FKKKSIKTRF KEIKQQINDD NRGSYESEEC RSQSTFSASS PRRSFVSAQE SIQMTPVPSP
LPREERFVTP EPFHRPTTRL SMEPTENLPS PEFGSLINNN RQINGKARFY RDYWKNVKVG
DFVRLYNNDQ IPADIVVLST SDSDGVCYVE TKNLDGETNL KIRYALHSGR KIKHARDCEK
AEFRIESEPP QANLYQYSGA AHWTQQSTAA DDELIEMSEA ININNMLLRG CNLRNTDWVL
GVVVFTGFDT KIMMNSGITP SKRSRISREL NWNVIYNFII LLLMCFVAAI IQGVTWAQGD
NSLNFFEFGS IGGHPALDGF ITFWAAVILF QNLVPISLYI SLEVIKTCQA FFIYSDSEMY
YAKIDYPCTP KSWNISDDLG QIEYIFSDKT GTLTQNVMEF KKATINGIPY GEAYTEAQAG
MQKRQGIDIV KEGARAREQI AQARIKMLNN IRKLHDNQFL HDDELTFIAP DFIADLAGES
TIEQQLANEN FMLALALCHT VISEIIPGDS TRIAFKAQSP DEAALVATAR DCGYTVLGST
PGNIRLNVQG HERNFKILNI LEFNSTRKRM SAIVRMSNNQ IVVFCKGADS VIYSRLKPGE
QVELRNTTAE HLEMFAREGL RTLCIAQKYL SEDEYRQWNR KYEKAAAAIQ DREEKMEFVA
DLIERDLLLL GGTAIEDRLQ EAVPDTIAVL AEAGIKLWVL TGDKVETAIN IGFSCNLLNN
DMELIVIKID DGEISTANEE LNKHLATFNM TGSDSELALA KNNHHAPPST HALVIDGDAL
KIVLDEQIRQ KFLLLCKNCK SVLCCRVSPA QKAAVVSMVK QGLDVMTLSV GDGANDVAMI
QEADVGVGIA GEEGRQAVMS ADYAIGQFRF LQRLILVHGR WSYRRLGETI ANFFYKNIVW
TFTIFWYQIF CSFDMTYLYD YTYILLFNLA FTSVPVIFMG VLDQDVSDKV SISVPQLYRR
GIERREWTQT KFWLYMLDGL YQSVVCFFIA YYLFYPANFV THNGLNVEDR ERFGVYIGPA
AVVVINTYIL LNTYRWDWLM VTLVVVSSLL VWFWTGVYSA FRTSGLFYKA AAEAFSQPSF
WAVTILSIIL ALLPRFCIKA AQKIYFPYDV DIIREQVRQG KFDYLHNPRQ PEDSIENLSH
TASSHNTYMA KEIQTSTVDE DQQPIYPPST TPSVTTHNTR NGSDGTDYIH HRQSLDVYSS
RLSMDRSRIS IDRPRPSFDR MRASMDKIRP SFEASSDFTS AARLARLNSS HSFNPLPSRI
NIPSGNS
//
