ID A0A4Z1PAN7_9PEZI Unreviewed; 1477 AA.
AC A0A4Z1PAN7;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=E6O75_ATG06815 {ECO:0000313|EMBL:TID19477.1};
OS Venturia nashicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Venturiaceae; Venturia.
OX NCBI_TaxID=86259 {ECO:0000313|EMBL:TID19477.1, ECO:0000313|Proteomes:UP000298493};
RN [1] {ECO:0000313|EMBL:TID19477.1, ECO:0000313|Proteomes:UP000298493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRI2 {ECO:0000313|EMBL:TID19477.1,
RC ECO:0000313|Proteomes:UP000298493};
RA Prokchorchik M., Won K., Lee Y., Choi E.D., Segonzac C., Sohn K.H.;
RT "High contiguity whole genome sequence and gene annotation resource for two
RT Venturia nashicola isolates.";
RL Submitted (APR-2019) 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 -!- 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:TID19477.1}.
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DR EMBL; SNSC02000012; TID19477.1; -; Genomic_DNA.
DR STRING; 86259.A0A4Z1PAN7; -.
DR Proteomes; UP000298493; 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; 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; 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:UP000298493};
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 86..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 479..502
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 527..548
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1099..1115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1127..1148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1178..1199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1219..1237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1244..1264
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1284..1304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 64..114
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1064..1313
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1477 AA; 166152 MW; 263978C23DF8F307 CRC64;
MSGTTDGEGG EGEGEGEGEG EGEAKGEEED GSENDESGED NGRRIFFNVP LPDDARDEDG
VALAQFPRNK IRTAKYTPIT FIPKNLWFQF HTVANIYFLF IIILGIFSIF GASNPGLNAV
PLIFILFLTA LKDAIEDWRR TILDNELNNA PVHRLVDFNN VNTAEDAISI WRRFKKANTR
AVLWVWRLWK AKKGAKGGKN YAQRALDESR PSVETTRPET GLSRPATRAS FHSVRSHSSD
NGEAIQMTPV PSPLPGQRPS TAEGSGHVKF PDYEDEIHPK NGSARQPAAP EVRTRYSGDV
INPNKQIPDK ARFKKDAWKN VQVGDFVRLY ENEEIPADMV VLSTADPDGA CYIETKNLDG
ETNLKVRTAM RATRNVKHAR HCEQAEFTID SESPHANLYG YSGVLKWTDY DRINPDSPPR
QMAEPITINN LLLRGSSLRN TEWVLGAIVF TGQETKTMLN AGITPSKRAK ISKDLNWNVI
YNFGILFLMC LVSGIVQGFT WARSDTSHAL FEFGSYGNNV PSLDGFITFW AAVILFQNLV
PISLYITLEI IRTLQAVFIY NDVEMYYAPI DYPCTPKSWN ISDDVGQIEY IFSDKTGTLT
QNVMEFKKAT VNGVPYGEAY TEAMAGMQRR QGINVEVEGA KARKQIDADR EIMFERLERL
HKNPYLRHED VTFIAPDFIS DLAGDGSREQ QDANAQFMLA LALCHTVIVE TSGGETPKID
FKAQSPDEAA LVATARDCGF TMVGRTDDKL VVSVQGVERR YQVLTTLEFN SARKRMSAII
RMPDDKIMLF CKGADSMIYS RLKKGEQAEL RQQTADHLEM FAREGLRTLC IAQKELDEDE
YQEWAILHDE AAASLVDREE KLEVLADRIE RDLTLIGGTA IEDRLQDGVP DAIQLLGRAG
IKLWVLTGDK VETAINIGFS CNLLDNEMDL IVFDIQDGDM ERAERELDNH LQTFNMTGSD
EELKAAQTNH EPPAPTHAIV IDGESLKLML DETLKQRFLL LCKQCKAVLC CRVSPSQKAD
VVKMVKDGLD CLTLAIGDGA NDVAMIQEAH VGVGIAGEEG RQAAMSSDYA IGQFRFLCRL
VLVHGRWSYR RLAETISNFF YKNLVWVFAL FWYQIYDNFD CAYVYDYTYI ILYNLAFTSL
PVILMGVLDQ DVSDKVSLAV PQLYRRGIER KEWTQPKFWI YMLDGLYQSV IVFYMTYLLF
APANFVTDNG LNIDDTKRIG VFIATIAVIV VNVYVLMNTY RWDWLMLLIV SISILLIWFW
TGVWTSTTSG FTFHGAAAEV YGQLNFWAVV LLTVIICLLP RFSFKAVQKI YFPLDVDIIR
EQVRQGKFDY LENSSSPVVD GAEKKADSLT SLSDGNGEAT DIKRKRTDAH MSEDLRPIYP
PSVAPTTTTR NRTTTGSDGT EYTNLSIDTA NTANNLDRSK TLERLERPIG PAMTPSVSRP
SFDRARMSMD RIRPSFEQSR DFTSASRLMR LESSCLA
//
