ID A0A395SEL3_FUSSP Unreviewed; 1443 AA.
AC A0A395SEL3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=FSPOR_3908 {ECO:0000313|EMBL:RGP70607.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP70607.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP70607.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP70607.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP70607.1}.
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DR EMBL; PXOF01000050; RGP70607.1; -; Genomic_DNA.
DR STRING; 5514.A0A395SEL3; -.
DR Proteomes; UP000266152; 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 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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF174; PHOSPHOLIPID-TRANSPORTING ATPASE DNF3-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 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:UP000266152};
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 374..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 418..441
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1237..1258
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1270..1290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1302..1326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1346..1366
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 91..145
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1123..1373
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1443 AA; 163559 MW; BEC212619306EC3E CRC64;
MSQDRPEVEA PLGPEPSKTN SKTNTRRRRS DAGQSAPLTN RIKDVAADLY QKTVVEFILR
RKHIVASTDG RHVPLELERE SPLIDDRRGL PYVSNSIRTS RYTVWDFIPK QLFFQFTRVG
NFYFLCVGIP QMIPGLSTTG SYTTILPLLF FVLLTIVKEG YDDYRRYRLD KIENAGFATV
LGREDKYTGK IKPVTKWRKW NPFLTNSTAE PHPAPNEEFN GLRWVPVRWS EIKVGDIIRL
CRDEPIPADL ILLDSDEENK LAYIETMALD GETNLKSKQV APALQGCDTI EGISKCKAEF
VVEDPNPDLY NFDGRVTVDE KTVPLTSNEV IYRGSIIRNT NAAIGIVINT GEDCKIRMNA
NKHPKAKKPA LEGVVNKIVV TLATYVVILS VGVSMGYVRW QKTTERHSWY LEQATVPFYQ
IIIAFIIMFN NVVPLALYIS LEIVKIGQLV MLNGDLKMYD EDTDTPARCN TNTILENLGQ
VGYIFSDKTG TLTDNIMKFR KISVAGTVWL HEMDLEQQVD EIEAIKLDEE SDPGEPSVYK
TEPVTVVIRE EQPEASHEPS TPLALPPTSH MSPRPSMSRR PSMAPSRPSM ALSRPSFGSR
RSSSQWRSTG RPDHIQPDVT TNDLIEYLRL RPNSGFAKKA KQYILAVALC HTCLPEHKDN
GELEFQAASP DELALVRAAQ ELGYLVISRT TQTITLRVTQ SDGQEEEQKY EVLDVIEFTS
SRKKMSIVVR FPDGRISVIC KGADSAILPR LKMSQVAKQK ANEVRKSADM EREIRRRSEQ
QEPRNSFGGR PSLTIRRNPG VSRDRSTSRR PNVDRSKSFE FGRLSRRSED KPRLSVATRG
VSIDMPRGQY LNTPVHYQQP VPDHLAFLED PALLDDSETF TKCFKHLDDF ATEGLRTLLF
AQRFITEQEY QAWKKVWDEA ATSLNNRQQR IEEAGDMIEQ SFDLIGATAI EDKLQKGVPE
TIERLRKANI KIWMLTGDKR ETAINIAHSA RICRPGSDLY ILDVSKGGLD SQLVALQEDL
QAGSVHSVVV IDGQTLSAVE NSPELSAKFF KVMLQVDSVI CCRASPAQKA LLVTTVRSRL
KKYRGKNRRG LTLAIGDGAN DLAMISASHV GIGISGKEGL QAARVADYAI AQFRFLQRML
LVHGRWNYVR TSKFILYTFW KEMFFYLPTA QYQRYTGYSG TSLYEATSLT VFNTLFTSLC
VICMGVWEQD LSAETLLAVP ELYVYGQRNQ GLNIWKFARW MLLGAIEGVI CWYGVWAGHG
WITPAVRDQG LYALGTLTFT AGVLWINWKL FIFETHYKSK IVIGSFFLTT IGWFAWLSFL
DAAYAPQPSG PYAIRDSFTT LFGDDAVWWA TLFIVLGLIG LFEIVLKCVK RLLLMHGLWD
WPPWGKSRRG ENIEEWDVEL WQELEQDPAL RARLKRMARD EPVEEEADVD LAQINIEEEI
RGR
//
