ID A0A2K1QV67_9PEZI Unreviewed; 1630 AA.
AC A0A2K1QV67;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-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=CAC42_6040 {ECO:0000313|EMBL:PNS18945.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS18945.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS18945.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS18945.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) 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:PNS18945.1}.
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; NKHZ01000036; PNS18945.1; -; Genomic_DNA.
DR STRING; 2082308.A0A2K1QV67; -.
DR InParanoid; A0A2K1QV67; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000243797; 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 PRINTS; PR00119; CATATPASE.
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:UP000243797};
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 535..558
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 578..602
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1326..1346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1373..1397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1409..1428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1440..1464
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1484..1504
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 281..338
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1262..1514
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1550..1570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1630 AA; 184160 MW; 67C11FF9AC4BEAE8 CRC64;
MAGDTRNNKH DEVRRRSTQS ERPQEHVQTG TTVIPALQRR ASDSANMSSS GTDLPAARNT
GESPRVRFST DVDRRPSLSK KHKNSDEVVP QLDTSKPPSP KLSLDVSGAH GGYTMGSPAS
IGSPEFGPPK SPRTGGRNRG LSLRSSIFQK NVRDRSADGR SVVEMNDMGS SSNSQHTQQR
STGKKSSATI VEIAPVDAPK YRDDISKADT KNIEGNLPAL PNYSNWLQRR AERTAGWRRV
KTTYQKVRKT ILRINEIPPS KDGRQIDLDP SRKDSFLDER TGKHYLGNTI RSSRYNIWNF
LPRQLWAQFS KLANFYFLVV SIFQVIPGLS TTGQFTTIVP LLFFVMLSIG KEGYDDLRRY
RLDKVENNQE TSVLKSVNDD EEPWKKVKWQ DIKVGDVIKL ERDEAVPADI VLLNSKGPNG
IANVETMALD GETNLKSKQV HPHLVKTCNS TSAIAHAGVH FVVEDPNLDL YNFEGKVTYQ
GNTAPLTNNE IIYRGSIVRN TPQATGMVIY TGEECKIRMN ANKNPRIKAP HLQQIVNKIV
IIIVIFVVAL SLFNTIAYQV WRGRVERPSW YLSNATVGFF PIMVSFIIMF NTMIPLSLYV
SLEIVKLCQM LLLNDIDMYD ETTNTPFEAR TSTINEELGQ ISYVFSDKTG TLTDNMMKFR
KISVAGTSWL HDVDLQPDGE GQHLLKHKNR KPKKSKGKKP MAQPRMSFNH PFEDNERTQK
HEGAHDDDHK LPRKSTSHWH SSARPDKAQP ELSTMVMIDY IQRRPHTTFA RKARMLLLSI
ALCHTCLPER DQNDEIEFQA SSPDELALVR AAKELDFIVF NRDASILTLK TFPHGKDAEP
VLEDYEILDV VEFSSKRKRM SVLVRFPDGR IAMFCKGADT IVMSRLRLAN LARQKANQIE
QRVNRRKSLE AHEALRRKSE QVEHGRPSNA RSSLSLGRKS FGAIGRTSMS AKLQPIRDEV
DSWLNEREHD VSAPPENVDE YYTPRPSMHA QRKQSLAASE MSSIHDGYDE ELVEDSLAAD
EEAVIERCFQ HINDFATEGL RTLLYAHRFL EDQEYDAWKK VYLDATTSLV DRQALIEKAG
ELIEQSLELT GATAIEDKLQ HGVPEAIDKL RRANIKMWML TGDKRETAIN IGHSCRLIKD
YSTVTVLDRE LGQLEQHIAA AILDVASGGI AHSVIVIDGQ TLANVESEPP LRKLFLDLAI
STDSVICCRA SPSQKSGLVK AIRRRVKNSI TLAIGDGAND IAMIQEAHVG IGITGREGLQ
AARVSDYSIA QFRFLVKLLL VHGRWNYVRV AKYTVGTFWK EIVFYLVQAI YQRYTGYTGT
SYYESWSLSL FNTLFTSLCV IFLGIFEKDL SAPTLLAVPE LYAKGQQNQS FNFMVYLGWM
FMGASESIII FFVSHALYGR SQFSTHQDID LFATGDIAFG ACIILINLKL QAIEIHNKSI
MALIANVASI GGWFLWNIIL AGVYQDNRIY FVRDGFTTRF GRNPVWWLTL VLAVTAALLF
ELAVRSVKAA YFPTDTETFQ MLERDPGVRR RFEEAAAMEL QMGWRSGRSS GEVRRQEEEE
RQREEEEKRA REVEELLRQR TGEDRGLGVD IGRVETEEER VVVEGIGRKS TDIAEMLSRR
FGTVKKDTLV
//
