ID A0A2L2T3W3_9HYPO Unreviewed; 1440 AA.
AC A0A2L2T3W3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Fusarium venenatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI64259.1, ECO:0000313|Proteomes:UP000245910};
RN [1] {ECO:0000313|Proteomes:UP000245910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA King R.;
RL Submitted (OCT-2014) 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}.
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DR EMBL; LN649229; CEI64259.1; -; Genomic_DNA.
DR STRING; 56646.A0A2L2T3W3; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000245910; Chromosome i.
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; 2.
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:UP000245910};
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 1234..1255
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1267..1285
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1297..1316
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1343..1363
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 1120..1370
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..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1440 AA; 163144 MW; B28C9A1CAFCC14DA CRC64;
MSQDRPDVEA PLGPEPSKTD SKTNTRRRRS DAGQSAPLAN RIKDVAADLY QKTVVELILR
RKHIVASTDG RRVPLELEHE SPLIDDRRGL PYVSNSIRTS RYTVWDFIPK QLFFQFSRVG
NFYFLCVGVP QMIPGLSTTG SYTTILPLLF FVLLTIVKEG YDDYRRYRLD KIENAGFATV
LGREDKYTGK IKPVTKWRKW NPFLTNSTAE PHPAPNEEFN GLRWVPVRWS EIKVGDIIRL
CRDEAIPADL ILLDSDEENK LAYIETMALD GETNLKSKQV AHALQVCDTI EGISKCKAEF
VVEDPNPDLY NFDGRVTVNE KTVPLTSSEV IYRGSIVRNT NATIGLVINT GEDCKIRMNA
NKHPKAKKPA LERVVNKIVV TLATYVVLLS VGVSMGYVGW QKSTERHSWY LEQARVPFYQ
IIIAFIIMFN NVVPLALYIS LEIVKIGQLI MLNGDLQMYD EDTDTPARCN TNTILENLGQ
VGYVFSDKTG TLTDNIMKFR KISVAGTVWL HEMDLEQKVD EIEAIKLDEE SDPGEPSVYK
TEPVTVVIRE EQSEGSHEPL ALPSPSHMSP RPSMSRRPSM APSRPSMALS RPSFGSRRSS
SQWRSTGRPD HIQPDVTTND LIEYLRLRPN SGFAKKAKQY ILAVALCHTC LPEHKDNGEL
EFQAASPDEL ALVRAAQELG YLVINRTTQS ITLRVTQSDG QEEEQKYEVL DVIEFTSSRK
KMSIVVRFPD GRISVICKGA DSSILPRLKM SQVAKQKANE VRKSADIERE MRRRSEQQEP
RNSFGGRPSL TIRRNPGVSR DRSTSRRPNV DRSKSFEFGR LSRRSEDKPR LSIATRGVSI
DMPRGQYLNT PVHYQQPVPD HLAFLEDPTL LDDSETFTKC FKHLDDFATE GLRTLLFAQK
FITENEYQAW KKVWDEAATS LGNRQQRIEE AGDMIEQSFD LVGATAIEDK LQKGVPETIE
KLRKANIKIW MLTGDKRETA INIAHSARIC RPGSDLYILD VSKGGLDSQL VALQEDLQAG
SIHSVVVIDG QTLSAVEKSP ELSAKFFKVM LQVDSVICCR ASPAQKALLV TTVRSRLKKY
RGKNRRGLTL AIGDGANDLA MISASHVGIG ISGKEGLQAA RVADYAIAQF RFLQRMLLVH
GRWNYVRTAK FILYTFWKEM FFYLPTAQYQ RYTGYSGTSL YEATSLTVFN TLFTSLCVIC
MGIWEQDLSA ETLLAVPELY VYGQRNQGLN IWKFARWMLL GAIEGVICWY GVWAGHGWIT
PAARDQGLYA LGTLTFSVGV LWINWKLFIF ETHYKSLIVM GSFFVTTIGW FAWLSFLDAA
YAPQPSGPYA IRDSFTTLFG DDAVWWATLF IVLGLIGLFE IVLKCVKRLL LMHGLWDWPP
WGKSRRGENI EEWDVELWQE LEQDPALRAR LKRMARDEPV GEEEDVDLAH LNIEEEIRGR
//
