ID A0A3N4L1Q7_9PEZI Unreviewed; 1171 AA.
AC A0A3N4L1Q7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=P167DRAFT_559019 {ECO:0000313|EMBL:RPB11905.1};
OS Morchella conica CCBAS932.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Morchellaceae; Morchella.
OX NCBI_TaxID=1392247 {ECO:0000313|EMBL:RPB11905.1, ECO:0000313|Proteomes:UP000277580};
RN [1] {ECO:0000313|EMBL:RPB11905.1, ECO:0000313|Proteomes:UP000277580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCBAS932 {ECO:0000313|EMBL:RPB11905.1,
RC ECO:0000313|Proteomes:UP000277580};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362033}.
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DR EMBL; ML119132; RPB11905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4L1Q7; -.
DR STRING; 1392247.A0A3N4L1Q7; -.
DR InParanoid; A0A3N4L1Q7; -.
DR Proteomes; UP000277580; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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 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; PF00122; E1-E2_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; 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:UP000277580};
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 133..154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1011..1033
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1101..1121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1127..1152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 116..166
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 951..1145
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1171 AA; 127626 MW; 47942A0CE1E2036B CRC64;
MGLGRRGVRR EELDEDEEAL LGGEHDDDDG GNNGRERDRE SLHGGNGGGG GGKRKLLRRL
SSRLSLRPGR IGGSGAGGAA AGGGDDAEPE TRVVGLGASG VAGVGGLKAL SKRKGKEAVY
PPNIISNHKF TPITFLPLTL YHEFSFFFNL YFLLVALSQC IPALRIGYLS SYIVPLVFVL
AITLGKEAHD DIARRRRDKE ANSELYEVLS FAPGTKRKNV GHLDDTLTLM KKSRDLKVGD
ILILKKDQRV PADVVILKTI SNEANSTDEE AASGETFIRT DQLDGETDWK LRLAPAPTQA
LRAGLLVGVT ITASAPSREV NNFVGSLAYE PHSIPEDENA ESSLASPSTP QAGFKVGLSI
DNTAWANTVL ASNSTTLAAI IYTGPETRAA LSTSRSRSKT GLLEKEINNL TKILCAITFS
LSIALVVLQA AEGHPAEEND GGNKPIQWYL QILRFLVLFS TIIPISLRVN LDMGKSAYAW
FIEHDKNIAG CVVRTSTIPE ELGRVEYLLS DKTGTLTQND MELKKIHVGT VSYAGEAMEE
VADYIKQGFL PGEAGAGSGT QSAVAVPSAA GGGGNTTRTR REIGTRVRDV VLALALCHNV
TPTTATEEGA SEATTTYQAS SPDEIAIVRW TESVGLRLVH RDRNGMRLVS VSTGEVVVRV
KILEVFPFTS EGKRMGIVVQ FIVNSHTTDL LSGPDEPSGD IWFYQKGADT TMSPIVQSND
WLDEECSNMA REGLRTLVVG RKKLSHSKYA EFSAAYKAAS LQLHSRDTQM ARVVEEYLER
DLELLGVTGV EDKLQKDVKS SLELLRNAGI KIWMLTGDKV ETARCVAVSA KLVARGQYVH
TIAKLKRKDL AYDALEFLRN KTDSCLLIDG ESLALFLSVY QTEFITLAVQ LPAVIACRCT
PTQKADIARL IRTHTQKRIC CIGDGGNDVS MIQAADVGVG IVGKEGRQAS LAADFSVEQF
CHLTKLLVWH GRNSYKRSAK LAQFVMHRGL VISVCQTMFS IASRFEPIAL YQGWLLVGYA
SVYTMAPVFS LVLDRDVDER LAELYPELYK ELTEGRSLSY RSFGVWVLVS IYQGSIIQGL
SQILVGLGDE NFERMVSVSH AYMIFAEVGT AVLFFASMPL LGEYFDLSYI VTIGFVWRVA
VISAISLIPP WVAKAVRRRL KPPSYAKVQG I
//
