ID A0A2K2DNA0_BRADI Unreviewed; 1057 AA.
AC A0A2K2DNA0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-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 Name=100838453 {ECO:0000313|EnsemblPlants:PNT75757};
GN ORFNames=BRADI_1g37700v3 {ECO:0000313|EMBL:PNT75757.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:PNT75757.1};
RN [1] {ECO:0000313|EMBL:PNT75757.1, ECO:0000313|EnsemblPlants:PNT75757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT75757.1,
RC ECO:0000313|EnsemblPlants:PNT75757};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:PNT75757.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT75757.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:PNT75757}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:PNT75757};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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 -!- 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; CM000880; PNT75757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K2DNA0; -.
DR EnsemblPlants; PNT75757; PNT75757; BRADI_1g37700v3.
DR Gramene; PNT75757; PNT75757; BRADI_1g37700v3.
DR Proteomes; UP000008810; Chromosome 1.
DR ExpressionAtlas; A0A2K2DNA0; baseline.
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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
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:SF150; 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; 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:UP000008810};
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 93..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 312..334
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 365..387
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 940..963
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 969..989
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 51..118
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 905..1000
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1057 AA; 118766 MW; 88F2CCEABCA1AE2B CRC64;
MARTGGRKRD RLRWSKLYTF SCFRTPSTDE AAGPSATNGS AVGGPGFSRI VHCNNSILHR
RKPLKYPTNY ISTTKYNVLT FLPKAIFEQF RRVANLYFLL TAILSLTPVC PFSPVSMIAP
LAFVVGLSMI KEALEDWRRF MQDMKVNNRK VSVHKGDGEF GYRHWEDLCV GDVVRVEKDQ
FFPADLLLLS SSYEDGICYV ETMNLDGETN LKLKRSLEVT LPLEEDDLFK DFRGVIRCED
PNPSLYTFVG NLEYERQVYA LDPFQILLRD SKLRNTSFIY GVVIFTGHDS KVMQNSTESP
SKRSRIEKKM DMIIYVLFTV LVLISLISSI GFAVRIKLDL PRWWYLQPQN SNKLDDPSRP
ALSGIFHLIT ALILYGYLIP ISLYVSIEVV KVAQAHFINQ DLHMFDEETG NTAQARTSNL
NEELGQVHTI LSDKTGTLTC NQMDFLKCSI AGVSYGVRSS EVERAAAKQM ASGAADHDIH
VEDVWENNED EIQLVEGVTF SVGKTQKSSI KGFSFEDDRL MHGNWTNEPN SSTVLLFFRI
LALCHTAIPE VNEATGALTY EAESPDEGAF LVAAREFGFE FFKRTQSSVF IREKHTSNGP
TEREFKILNL LEFNSKRKRM TVILKDEDNR IVLLCKGADT IIFDRLAKNG RLYEPDTTRH
LNEYGEAGLR TLALSYRVLE ESEYASWNAE FLQAKTSIGP DRELQLERVA DLIEKELILV
GATAVEDKLQ TGVPQCIDRL AQAGLKIWVL TGDKMETAIN IGYACSLLRQ GMKRISLSTT
AGDQVAQDAQ KAAKESLMLQ IANGSQMVKL EKDPDAAFAL IIDGKALTFA LEDDMKHMFL
NLAIECASVI CCRVSPRQKA LVTRLVKEGL GKTTLAIGDG ANDVGMIQEA DIGVGISGVE
GMQAVMASDF SISQFRFLER LLVVHGHWCY KRIAQMICYF FYKNITFGLT IFYFEAFAGF
SGQSVYDDWF MLLFNVVLTS LPVISLGVFE QDVSSEICLQ DGWGMASTHL WRYSFSTSVS
SMIKQSVPGD RHLIWPQLEL PCSPASSGLS TFRLLSR
//
