ID A0A507F8G3_9FUNG Unreviewed; 2117 AA.
AC A0A507F8G3;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=P-type phospholipid transporter {ECO:0000256|ARBA:ARBA00012189};
DE EC=7.6.2.1 {ECO:0000256|ARBA:ARBA00012189};
GN ORFNames=CcCBS67573_g05740 {ECO:0000313|EMBL:TPX72579.1};
OS Chytriomyces confervae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC Chytriomycetaceae; Chytriomyces.
OX NCBI_TaxID=246404 {ECO:0000313|EMBL:TPX72579.1, ECO:0000313|Proteomes:UP000320333};
RN [1] {ECO:0000313|EMBL:TPX72579.1, ECO:0000313|Proteomes:UP000320333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 675.73 {ECO:0000313|EMBL:TPX72579.1,
RC ECO:0000313|Proteomes:UP000320333};
RX PubMed=31209237; DOI=.1038/s41598-019-45128-9;
RA van de Vossenberg B.T.L.H., Warris S., Nguyen H.D.T.,
RA van Gent-Pelzer M.P.E., Joly D.L., van de Geest H.C., Bonants P.J.M.,
RA Smith D.S., Levesque C.A., van der Lee T.A.J.;
RT "Comparative genomics of chytrid fungi reveal insights into the obligate
RT biotrophic and pathogenic lifestyle of Synchytrium endobioticum.";
RL Sci. Rep. 9:8672-8672(2019).
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 -!- 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}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109}.
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:TPX72579.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QEAP01000217; TPX72579.1; -; Genomic_DNA.
DR STRING; 246404.A0A507F8G3; -.
DR Proteomes; UP000320333; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
DR GO; GO:0009100; P:glycoprotein metabolic process; IEA:UniProt.
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; IPR007074; LicD_fam.
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; PF04991; LicD; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000320333};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 710..731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1025
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1045..1069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1607..1626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1638..1655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1685..1703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1723..1742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1749..1770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1790..1808
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 667..718
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1575..1818
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 770..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2052..2117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2087..2105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2117 AA; 237233 MW; 7B8DA71420D3CF84 CRC64;
MSTQPPQQQQ QRRHRSQLAL AAGVTVTLLL GLAPLLSVQT LPSFASTNRV SSDKSNDWQQ
FSAEIALNAA IIEVESVDAS DAAVQPEIGP ASVDVESDSA HSFPPSPAAD KISDPLVEPA
ASKLGQAKFE FTPTPVTPAT NKDKEYKAVV SFHGKSFISN LDLHTASYNG ISPYYENTTF
LNTPIVSGEK STLALARMAS YDTGKLVTIP RSHFNLSQPS PNVPSFNPEQ AIVTAILDKK
YFYECGADLK RDYRYTKPED CQINNKVPSA NSMESNILHN LQYAQLSVKS LMKAWIDFSQ
KNSIVWWVSH GELLGWAWNG NLLPWDLDWD LQMTTYQLVQ LVAFNQTLID GRFFIDVNPS
IYVRTRQPNN IIDARVIDTW TGYFVDITGV SYLDRTLMNK DFHQITYAWN EAEEKNRFNE
TDPQRIYCKS IHRYSYDDLM PLHETMLAGL KVWRPRAALK LIVREYSENA LIKEKYAVGN
REEVYAWDRK AAQWSLTKTK SKNQPYRWGA NARADEMETA QVVDQPGSTA TATLSESSLP
DMYVNLNNYN SSRDPEFTTC PNPIQRTVRE SNAPESVFAY ATGAVSFKKD HQNCGAGSSN
LFIFQMPKQK VNWLGSRSNV DVMDLAADEA LKTTAVKPTK RRILINKPTL DKTTAAAAAV
ESGSVGASNK VTTSKYTVLS FLPKNLFEQF RSIANFYFMS LVVLQAFPPF MLVSTILTAT
PILIIVFATM IKDAVEDWRR HVSDENVNHA KTHKLYNVRN WNFPLSNLPS SKSHSSHPPS
SHIQIPNADI NSTKSTMPSS STFKIQSYPY KMPGIRASIT SHENPHELEE PPYWAENTWE
NVRVGDFVYL CNNENIPADV LIVSSSEQDA TCYIETKNLD GETNLKIRRG LNEFAHIQSP
ADCAALVGVI DSELPSANLL TYNGVIQVQS SGANPLTSLK GPDTSKTLSI GMNNMLLRGC
ILRNTKWAIG IVIYTGADTK IMLNSGTTPS KRSKIDRQLN PLVMLNFWLL GAMCLICALI
SAVYTATFIH EDALFAPNAG QYTPLYAAFI AFFSCLIIFQ NIVPISLYIS VDVSKTVQSL
FISMDLDLFD DETGKFAGPR SWNLSDDLGQ IEYIFSDKTG TLTCNMMEFR KCSINGVVYG
GSYKAATELS NGNSVNTKDN TMQEARKVME TDMRNELGRV FDTKYLSENL SFVDTVLPRH
LQENGEQARK IREFFTLLAV CHTVLVEKPD GDEKPNHIEY RAQSPDEAAL VAAARDVGFA
FLKRQDDLAE IDLMGASRTY KIMNILEFNS DRKRMSVIIK RPEGQLVLLV KGADSVIFER
LAKTEDGDPD SALQLATAKH LEAFANQGLR TLCLAYKIIP NYEYEAWEEQ YRDAQNSVHN
REKNVDAAAE LIERDLTLMG ATAIEDRLQD GVPETIATLS KAGIKIWVLT GDKMETAINI
GFSCNLLKKK MLLIVINSTS LKDTYTQLMD ALEKFWTPEG VPVREEKLAL IIDGTSLKFA
LMACCRPLLL EIGCRSQAVI CCRVSPLQKA RVVSLVRKGL GAMCLAIGDG ANDVSMIQEA
DIGVGISGKE GLQAVMASDY AIGQFRFLGK LLLVHGRWGY VRTAEIIFNY FYKNAVWLFT
LLWYQFDSDL ITDFTYGMFF NTMFTLFPTM FIGFYEQDLN AGICVQVPQI YRKGMKQTVF
NIERYWVYMF DALWQSIIAY FFVRDMYDGS APYMTGHAGD HESMGTMISF ICIICTNLHA
VINTTNWTYL TFFGLFASYA VWLFYVISYA RSSDNASYGQ LETLYLEPHF YLGITMSVVV
ALLPRFVLKF AQQYLAPTDS DILLEYQKYH WREGSTIPNM DLESQTPYRE SVVDNLHTEE
QVRLLEPNDS SPLKSVGSDN AFEMSRKSEH RVASKAISIH RSQSEKSVAA LSERAVLDNS
GKNFTVKDEF ARLLASRNFA PPTIPYKKNK MVRRSVAGLD DFKIKSPDGF APIAKRRQKS
ETVLRHSSEW NTIDAMNEPQ EMKQSPPPPS SASRLGVTKT SIFFMGTQEE LPNTGFCFSH
EEGMTDLIKP SQQSKSRFEL DGGPSSAGYS GFEARVRNAS AMQMRRDANP AGSSSRVGSR
PSIRRSQSLH HSDSKKK
//
