ID A0A2W1FKD7_9PLEO Unreviewed; 1343 AA.
AC A0A2W1FKD7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=Ptr86124_008773 {ECO:0000313|EMBL:KAI1511933.1}, PtrM4_12790
GN {ECO:0000313|EMBL:PWO07063.1}, PtrM4_129150
GN {ECO:0000313|EMBL:KAF7568302.1};
OS Pyrenophora tritici-repentis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=45151 {ECO:0000313|EMBL:PWO07063.1};
RN [1] {ECO:0000313|EMBL:PWO07063.1, ECO:0000313|Proteomes:UP000245464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4 {ECO:0000313|EMBL:PWO07063.1,
RC ECO:0000313|Proteomes:UP000245464};
RX PubMed=29685100; DOI=10.1186/s12864-018-4680-3;
RA Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P.,
RA Moffat C.S.;
RT "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici-
RT repentis reveals chromosomal variations and genome plasticity.";
RL BMC Genomics 19:279-279(2018).
RN [2] {ECO:0000313|EMBL:KAI1511933.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1511933.1};
RA Moolhuijzen P.M., Moffat C.S.;
RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAI1511933.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1511933.1};
RA Moolhuijzen P., See P.T., Shi G., Powell H.R., Cockram J., Jorgensen L.N.,
RA Benslimane H., Strelkov S.E., Turner J., Liu Z., Moffat C.S.;
RT "A global pangenome for the wheat fungal pathogen Pyrenophora tritici-
RT repentis and prediction of effector protein structural homology.";
RL bioRxiv 0:0-0(2022).
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:PWO07063.1}.
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DR EMBL; NQIK02000007; KAF7568302.1; -; Genomic_DNA.
DR EMBL; NRDI02000012; KAI1511933.1; -; Genomic_DNA.
DR EMBL; NQIK01000012; PWO07063.1; -; Genomic_DNA.
DR Proteomes; UP000245464; Unassembled WGS sequence.
DR Proteomes; UP000249757; 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 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; 2.
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 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 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 284..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 486..507
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 535..556
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1047..1067
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1087..1109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1130..1154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1166..1183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1195..1220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1240..1257
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 221..287
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1016..1268
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1343 AA; 150238 MW; 96B12B4FB78B1985 CRC64;
MASRPPGGPS HSENLIDFDD HQPTHNAGAP PRPAAHDEGR PSVSYDDFVG GARSTTAGLP
GGPGAPGGAT TPYLGGANNN SRAYSQTSDL HNYQRYSDAD IPHDDDASTQ GYYAAGGAYD
QPSPSLQRGN SKNAHNRNSI LSLGGGLTGR VKNMFGRGNE YSEMDLPLTE NAAHQRQPSG
NETASQHDDG HSAKPKKGLG TFKFGFGRGT PDPSTLGPRI IHLNNPPANA VNKYVDNHIS
TCKYNIVTFL PKFLYEQFSK YANLFFLFTA ILQQIPGISP TSRFTTIVPL GIVLLVSAVK
EYIEDYRRKQ SDSELNNSKA QVLKGSTFTD TKWVNVAVGD IVRVESEQPF PTDLVLLASS
EPEGLCYIET ANLDGETNLK IKQAIPETAD YVSPAELARL GGRIRSEQPN SSLYTYEATL
TIAAGGGEKE LPLAPDQLLL RGATLRNTPW IHGVVVFTGH ETKLMRNATA TPIKTTAVER
MVNKQILMLV LILIALSIIS SIGDVIIQTT QRDSLVDYLR LDRFNGAKQF FRDLLTYWVL
YSNLVPISLF VTIEIVKYYT GSLIDSDLDI YYEPTDTPAK CRTSSLVEEL GQIEYIFSDK
TGTLTCNMME FKQSTIAGIQ YADEVPEDRR GTIEDGVEVG IHDFKQLEQN RKTHHNKYII
DQFLTLLATC HTVIPERKGE KAAIKYQAAS PDEGALVEGA VTLGYKFTAR KPRAVIIEVD
GRELEYELLA VCEFNSTRKR MSTIFRTPEG KIVCYTKGAD TVILERLGKD NPHVEATLTH
LEEYASEGLR TLCLAMREIG EDEFREWWTI FNTAQTTVGG NRADELDKAA ELIEHDMTLL
GATAIEDKLQ DGVPDTIATL QSAGIKVWVL TGDRQETAIN IGMSCKLISE DMSLLIINEE
NKEDTRDNIR KKFQAITSQS QGGAEMDVLA LVIDGKSLTY ALERDLEKEF LDLAVKCKAV
ICCRVSPLQK ALVVKLVKRH LKSILLAIGD GANDVSMIQA AHVGVGISGV EGLQAARSAD
IAIGQFRYLR KLLLVHGAWS YQRVSKVILY SFYKNIAMFM TQFWYSFQNG FSGQIIYESW
TLTMYNVFFT AAPPFVLGIF DQFVSARLLD RYPQLYRLSQ SGVFFRMHSF WSWVGNGFYH
SLILYFGTQA FVLWDWPQWD GRNAGHWVWG TAAYTANLAT VLLKASLITN IWTKYTVLAI
PGSMLLWFIL MPLYATVAPM INISNEYVGV IARLFPDPRF WAMIVVLPPL CLIRDFAWKY
AKRMYFPQSY HHVQEIQKYN IQDYRPRMEQ FQKAIRKVRQ VQRMRKQRGY AFSQTDESQA
RVLQAYDTTQ QRGRYGEMAS SRK
//
