ID A0A1V6T7N1_9EURO Unreviewed; 1634 AA.
AC A0A1V6T7N1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=PENFLA_c013G02552 {ECO:0000313|EMBL:OQE22186.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE22186.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE22186.1}.
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DR EMBL; MLQL01000013; OQE22186.1; -; Genomic_DNA.
DR STRING; 254877.A0A1V6T7N1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000191342; 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:UP000191342};
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 541..563
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 583..602
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1309..1329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1359..1381
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1393..1410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1422..1441
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1469..1489
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 271..329
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1245..1499
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1634 AA; 183607 MW; F89B40769CF26B00 CRC64;
MSNDKSTEPT EGSQPEQNDA LRRPSLVPSR TLSDSGRRIS SQHVRFSTDL DRESAEEQRQ
TNWDGRPNSR GLTINTALAP PSVRAAPSPT SPLSPRNATL SPIPPPSPES AGRSRSRNRG
YSLRRTIFNK TINSTEKDDL ALAELGEAKE PSSNVTPAQT PAAETLTAAD EKHALSVAPT
ATLDSTHKED ASPYVSSEPS EKGLKEQFSV SVAHEKWLQK KATTAVAVAR FQAVMTSIQK
FILRIKDIPP TKDGRHIDLN PSMVGSMIDE RTQKPYIGNY IRSSRYSLWS FFPRQFFAQF
TKVANFYFLI VAILQMIPGL STTGTYTTIV PLLIFVGISM GKEGFDDWRR YRLDKEENNR
DAWVLRQGHG TIQDGASMIS NAQDWERIKC EDIRVGDVIK LERDQPIPAD IALLHASGPN
GVAYIETMAL DGETNLKNKQ PCQPVSKVCS TVEDINNNSL HFVVEDPNLD LYKFDGHVSV
NGQEKLPLTN NEIVYRGSIL RNTDRALGMV IYTGEECKIR MNANKNPRIK RPALQDKVNR
VVMLIVVLVV ILAVICTVSY KYWSQDVEQH SWYLEDASVS YGPIFTSFLI MFNTMIPISL
YVSMEIVKVA QMLLLNDIDM YDPETDTPLE ARTSTINEEL GQVSYIFSDK TGTLTNNSMR
FRKMSVAGTA WLHDADLQEE AARAGDHTKL IHKKRSTKGK KAMGRKSNVS EAQMPRPSNV
SGPLDAFRQS GRSATTYRTE EMLEYIQRKP YTIFARKAKL FILSMALCHT CIPEEDANGN
TTFQASSPDE LALVLAAQEL GYLVVDRQSN TLTIRTQPNG PDEATSDEVY EVMDVIEFSS
ARKRMSVVVR MPDQRICLFC KGADTTLMRL LKQADLAHEK ATEIERRASR RKNAEMNQVI
RRNSEHHSRK NSGARSSMTR PSFNRRRSSI TGQQGSALRA SIDVWLRDRE TDGGMRYREA
DSEYYSPRPS AQMGRPSAAI SDSGSSTNGE DDEDLVEEAL VVNEAAIFER CFQHLNDFAT
DGLRTLLYGH RFLDEATYTN WKTAYNEACT SIVDRQQKIE DAGEQIEQQL ELTGATAIED
KLQKGVPEAI DKLRRANIKM WMLTGDKRET AINVGHSCRL VKEYSTLTIL DHENGDVEQS
IAHLIGEITR GRVAHSVVVV DGQTLSLIEA NEVVREQFFQ LAVKVDSVIC CRASPKQKAF
LVRSIRKQLT DAITLAIGDG ANDIAMIQEA HVGIGITGKE GLQAARISDY SIAQFRFLLK
LLLVHGRWNY LRACKYTLGT FWKEMLFYLT QALYQRWNGY TGTSLYEPWS LSMFNTLFTS
LAVIFLGIFT KDLSASTLLA VPELYTKGQR HGGFNIRLYL GWSFMGTCGA VIIFFTMWSL
YGLARVNPSD NDIFSLGLLT YSACIIVINM KLQVLEVHNK TYLSLIVVII SVGGWFMWDL
ILDREYTMSS GKGIYFLPSN FIHHSGHNLL FWTVLFLSVS AVLLFEFTVS TLRALFFPTD
VDIFQEYEQD LDIRKRFEEA AASELQQGWD HGTKRSSFEI ARENAEKAEM DARERQVREL
LARPRVMDTK ELEVDTASAT VSHNSSVPSH NAETDRGRQS GLLCPEDANG RRRSVEIQEL
FSKGYGAVRK GQLK
//
