ID A0A232LU47_9EURO Unreviewed; 1284 AA.
AC A0A232LU47;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=Egran_04582 {ECO:0000313|EMBL:OXV07652.1};
OS Elaphomyces granulatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Elaphomycetaceae; Elaphomyces.
OX NCBI_TaxID=519963 {ECO:0000313|EMBL:OXV07652.1, ECO:0000313|Proteomes:UP000243515};
RN [1] {ECO:0000313|EMBL:OXV07652.1, ECO:0000313|Proteomes:UP000243515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSC145934 {ECO:0000313|EMBL:OXV07652.1,
RC ECO:0000313|Proteomes:UP000243515};
RX PubMed=25753751; DOI=10.1111/1462-2920.12840;
RA Quandt C.A., Kohler A., Hesse C.N., Sharpton T.J., Martin F.,
RA Spatafora J.W.;
RT "Metagenome sequence of Elaphomyces granulatus from sporocarp tissue
RT reveals Ascomycota ectomycorrhizal fingerprints of genome expansion and a
RT Proteobacteria-rich microbiome.";
RL Environ. Microbiol. 17:2952-2968(2015).
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:OXV07652.1}.
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DR EMBL; NPHW01004652; OXV07652.1; -; Genomic_DNA.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000243515; 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; 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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 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; 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:UP000243515};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, 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 205..225
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 231..248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 552..571
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1082..1102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1108..1130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1155..1174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1180..1200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1207..1229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1249..1270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 174..224
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1048..1276
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1284 AA; 142299 MW; 633B8F3D5C316A50 CRC64;
MSLATEYLHG VDMDTLPSGS DSEDDLDLEE LDPQSTEISS NARRYKEDHN EIRGFGTRIA
MRNLRTGARG RLWKQETPGY HRRSEEDFSD LLDDRSDKQQ LSQGSSNPNE DNIPLLRNHR
RGGSPLPEPK VAKQWLTFGG MLGLPSFRST SETQTSPDTS SDSKPVRSIL AGQSQDYKFP
ANLVSNAKYT AWSFLPRTLY NEFSFFFNMY FLLVALSQII PVLRIGYISS YIAPLAFVVS
VSLGKEAYDD IGRRRRDAEA NSEEFTVLSF GRRATKSPRI YSRAPSMPSS QDPDTTGITE
VTKKSRDLKV GDVLKIRKDQ RLPADVVILR SIATEKATSK LRVSSNEESS QEPVGGVLDA
VEDGSVVQSD VQSRFGTDST SDTFIRTDQL DGETDWKLRF PPALSQNLPL SEFTRLKITG
GAPDCKVNEF VGKIELVPSS SNAYDPSIGK LQPSNDETLR AGAPQNDSVA LTIDNTAWAN
TVLASNTTTL AVILYTGPQT RSALSTSPSR SKVGLLEYEI NSLTKILCIL TLTLSFTLVA
LEGFQPTNDK PWYIAIMIYL ILFSTIIPMS LRVNLDMAKT VYARFIERDR GIPDTIVRTS
TIPEDLGRIE YLLSDKTGTL TQNEMELKKI HVGTVSYANE AMEEVALYIR QGFANHTAAD
STQPSLITPS SVFPGHSAAA RTRREIGSRV RDLVLALALC HNVTPTMGEE DGHKVTSYQA
SSPDEIAIVK YVEGLGLRLA YRDRQSIILE SSDRNQIVVR VRILEIFPFT SESKRMGVIV
QFEQDAGAPD LSKNDSDIWF YQKGADTVMS SIVAANDWLD EETANMAREG LRTLVVGRKK
LSTAQYQQFS ADYKQASLAL QGRDAGMATA VSEYLERDLE LLGVTGVEDR LQRDVKPSLE
LLRNAGIKIW MLTGDKVETA RCVAISSKLV ARGQYIHTVT KLQDRSTAQN TLDFLIHKTD
ACLLIDGESL SIMLSQFRLA FISIAVLLPV VVACRCSPAQ KAEIADLIRQ HTKKRICCIG
DGGNDVSMIQ AADVGIGIVG KEGRQASLAA DFSITQFHHL TKLLVWHGRN SYKRSAKLGQ
FIMHRGLIIS ACQTMYSIAS HFDPKGLFIN WLLVGYATVY TNAPVFSLVL DRDVDEELAN
LYPELYKELK TGRSLSYRSF FTWVLVSVYQ GAVIEGLSQI LVGAVTGPRL ISVSFTALVL
NELMMVAIAV TTWHPVMIFS LLGTVLLYAA NVPFLGDYFD LEFVITIGWL WRVAAVLAVS
LVPVWVGKLV KRVWSPPSYR KVQG
//
