ID A0A2A9NV81_9AGAR Unreviewed; 1380 AA.
AC A0A2A9NV81;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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=AMATHDRAFT_141843 {ECO:0000313|EMBL:PFH51676.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH51676.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH51676.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH51676.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) 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}.
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DR EMBL; KZ301985; PFH51676.1; -; Genomic_DNA.
DR STRING; 703135.A0A2A9NV81; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000242287; 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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF153; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_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 SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000242287};
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 106..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 359..380
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1034..1053
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1065..1086
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1116..1138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1150..1170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1182..1203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1223..1242
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 50..111
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1002..1252
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 508..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 756..787
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1288..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 155596 MW; 0040DBF876D5120B CRC64;
MPPPKSSFTR FYERLVAFNV ESLFTRKRAP GPPRTVYVNQ PLPAEFLDHK GRVKPEHVYT
PNQVITSKYA IITFIPRNLL EQFRRVANMF FLALAIIQFF PTFTTITPGV AILPLLFIIA
VTGLKDGYED FKRHQSDKRV NYSTVRVLEG GGWNNPNAMQ PKRKTFIRGL LPTGSSPQRG
PDIEFDDVSD SDGIYGDKNM RPHWKKTLWE DVRVGDFVKL VEGESFPGDI MICATSEEED
VAFVETKNLD GETNLKSRHA VPTLIHLRTA ADCADAKAFK INCDRPDNDM YRLNANVDYD
GVKTPVDLSM TLLRGTLLKN TSWVIGIVMF TGLDTKIVMN SGNTPSKRSR VERQMNPQVF
LNLGLMAVMA VVCAIVDSVL ETRYYPLGAP WLYGDDRGGD NPRINGLITW AYAILTFQDI
VPISLYISIE FVRTCQAIFI YLDPDIWYRK TDQPTIARSW NLSDDLGQIE YIFSDKTGTL
TQVRGNLFYF HYNLMVFRQC SVGGKAYRGA SSNEPVEDDP DFTPQVSRYP ASTEKLDNSF
STAQWEAKAK PSGSSYQLSL TDGPSRPASD DDGDDVVHFH DSELQQDLEL AVTVDETSEF
ASHARSLNGF FTVLSLCHTV LTGEDPETGN IIYKAQSPDE AALVQAAADV GFVFLGRDRE
ILRLRTPFSP EIEQYELLNI LEFTSARKRM SVILRKLGED PRIFLLTKGA DNVIFERLRA
GGDDLKAITD RHLGEFANEG LRTLTLAYKV IRDEVYEAWN LRYRQANAEL DDREEKVEAV
CDEMERDFRL LGATAIEDRL QDGVPETIAD LKRAGIKIWV ATGDKLETAI AIGRSTNLIT
PDSNIVIIRG SNKRSAYEQM TIALQQYFSD FGGKESSGPE AQYRNNDPEI PLQRIMTGVS
SIVGEGNGER DGGFVLVVDG AALLEAFATD ENRDLLLRLG TKCDAVICCR VSPLQKALIV
RLVKEGLKTM TLAIGDGAND VSMIQAADVG IGISGEEGLQ AVNSSDYAIA QFRFLKRLLL
VHGHWSYARN GTMILNFFYK NIMPVGVLWW FQIYSAWSGY YGFDYIYILF WNSLWTILPV
IGIGLFDRIL DDEILMQFPE LYRYGRTGYW YNTKYFCIYM FDGIVQTVII FFFIFYSYIS
PTSRPDGFQI NMVELSSTMV FSAVLTADIF AGITSTAWTI PLVIAIAFGI IVIWCFTAIY
SLVPPTYAPT NLWGLDEFIF RSAYFWLGLL LTFVLAISPR IIAKAWKISF FPDEIDIIRS
KLKEDPHFDL SQLRLGLERF KRPPSRPFSR SSMRSPGPTQ DVRMASRTDM ATGLASVDRG
FDFVTEEGGV AMRRMQSRLS EQKVPQRRSS PKKGKGTISH VFSLRRGLLR KSASILRKSE
//
