ID A0A6G1C1P9_9ORYZ Unreviewed; 951 AA.
AC A0A6G1C1P9;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
DE Flags: Fragment;
GN ORFNames=E2562_031422 {ECO:0000313|EMBL:KAF0893887.1};
OS Oryza meyeriana var. granulata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza meyeriana.
OX NCBI_TaxID=110450 {ECO:0000313|EMBL:KAF0893887.1, ECO:0000313|Proteomes:UP000479710};
RN [1] {ECO:0000313|EMBL:KAF0893887.1, ECO:0000313|Proteomes:UP000479710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Menghai {ECO:0000313|Proteomes:UP000479710};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF0893887.1};
RA Li W.;
RT "Whole genome sequence of Oryza granulata.";
RL Submitted (NOV-2019) 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 -!- 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:KAF0893887.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SPHZ02000011; KAF0893887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G1C1P9; -.
DR Proteomes; UP000479710; 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: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 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; 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:SF199; 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; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 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:UP000479710};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..951
FT /note="Phospholipid-transporting ATPase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026063086"
FT TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 769..787
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 799..818
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 851..871
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 883..903
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 909..931
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 735..950
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAF0893887.1"
FT NON_TER 951
FT /evidence="ECO:0000313|EMBL:KAF0893887.1"
SQ SEQUENCE 951 AA; 106389 MW; 9737DD904EEE8D59 CRC64;
RFMNQYFLLI ACLQLWSSIT PVSPATTWGP LAIIFIVSAS KEAWDDYNRY LSDKQANERE
VWAIKDGSHR QIKAQDIHVG NIVWLHQNDE IPCDLVLIGT SDPQGICYVE TAALDGETDL
KTRIVPSTCA NLSPEQLGRV KGVVECPNPD NDITRFDANM CLAPPIIDNE KCPLTINNTL
LQSCYLRYTE WACGVAVYTG NETKSGMSRG TAEPKLTAAD AMIDKLTVAI FVFQVVVVLI
LGFAGNIWKE NQGLKQWYLM YPAEGPWYDF LIIPLRFELL CSIMIPISVK VTLDLAKGVY
AKFIDWDEQM FDWETCTPAH SANTAISEDL GQVEYILSDK TGTLTENRMI FRRCCISDTL
YGENNGDALK DARLLDAVSS NDPDVVKFLM VMALCNTVVP IKSNDGTITY KAQSQDEEAL
VTAASKLNMV LVNKDSSTAE ISFNDSKFHY NLLDILEFTS DRKRMSAVVK DVQSGKILLL
SKGADEAILP RSHQGQQIRT YLEAVEMYSQ LGLRTLCLGW RELEEDEYKD WSKTFQDASC
SLENRECKIA EVCNSLEQDL HILGVTAIED RLQDGVPETI KLLKSAGINV WMITGDKQNT
AIQIGLLCNL IAPEPNSQLL SINGKTEDDV LRSLERALST MKSMTVTKDC AFVLDGWALE
IILKHSKESF TKLVMLSRTA ICCRMTPLQK AQLVGLLKSV GYLTLAIGDG GNDVRMIQEA
NIGVGISGRE GLQAARAADY SIGKFKFLKR LILVHGRYSY NRTAFISQYS FYKSLLICFI
QILFSFLSGL SGTSMFNSIS LMAYNVFYTS LPVMTIIFDK DISEATVLQY PQIFLYSQSG
RLLNPSTFAG WFGRSVYHAL VVFLTTIIAY AGEKSEMEEL SMVALSGCIW LQAFVVTLDT
NSFTYPQVIL IWGNFVAFYM INLIVSAVPT LQMYTIMFRL CSQPSYWITM A
//
