ID D8M5K7_BLAHO Unreviewed; 985 AA.
AC D8M5K7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=GSBLH_T00003235001 {ECO:0000313|EMBL:CBK23346.2};
OS Blastocystis hominis.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=12968 {ECO:0000313|EMBL:CBK23346.2};
RN [1] {ECO:0000313|EMBL:CBK23346.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore isolate B {ECO:0000313|EMBL:CBK23346.2};
RA Wincker P.;
RT "Sequencing and annotation of the Blastocystis hominis genome.";
RL Submitted (FEB-2010) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362033}.
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DR EMBL; FN668661; CBK23346.2; -; Genomic_DNA.
DR RefSeq; XP_012897394.1; XM_013041940.1.
DR AlphaFoldDB; D8M5K7; -.
DR EnsemblProtists; CBK23346; CBK23346; GSBLH_T00003235001.
DR GeneID; 24920343; -.
DR InParanoid; D8M5K7; -.
DR OMA; GSIIVWY; -.
DR OrthoDB; 102669at2759; -.
DR Proteomes; UP000008312; 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; 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:SF91; 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 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:UP000008312};
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 77..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 345..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 41..105
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 863..910
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT COILED 618..645
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 985 AA; 111473 MW; 03CE034AE65C25A1 CRC64;
MARSYINIHE SRRTFENHLH SQRKKQQSDE ARLQAYMLLN VFLNRRDQNK DRFPRNVFIT
SKYTPWNFLF INLFEQFSRV ANFVFLLVTL VQLIPGVSPF NIWSTLLPLI FILLVTAIKE
AWEDYLRHKA DKITNNVMYK RILPDGSMQQ IPSCEIVPGD VIVLEDQEAI PADILVLACS
DSDGTCYVDT SSLDGETNLK EKQAVSLTKK VDSPSALGQI NGTLTCQIPT KELSVFQGIF
AVKPEGGGND LEESVDSKNL LLRGSILKNS NWVAGMVVYT GRLTKLSLNM NISKFKFSGI
ETSLNSFVPK VLFLQLALTL VCRARSFGHR FAAAARESIR PLYDWLFDFF TFFILFSYFV
PMSLYVVFEF SRTLQAFFME NDLDMYVENE GGMHVSTSSL NEELGNVEFI LSDKTGTMTK
NNMQCFGFSM GGIEFIDSDF PTPLPEGVSV ESLLRKRNQG NELSNLEREY VLNFLRAIFL
CNSIKPVEQD GRTVLRAESA DEEALLSGGM KLGWELLLRT KDTVIIREGY PSSPDESAQD
GVHKFELLEE LPFTSSRQRM TILVRDTWNN KICLYSKGAD SKMLSLSCDE EEMVKYGVGE
MAESLYKQGY RLLLVGGKYV LESELEEWEH ELDKAKKSMK HREENIEKAF VYIERDLSIL
GATAVEDELQ DCIREDIQLL REAGITVAMA TGDKKETAMI IARNCGLLTD SMQLFDLTGS
KEHVALQLDA ALEHSHYKQH LRIQEYNAKN QKWSQRLLQL CSTRRSNASP RLDPYAPFAL
ILDGISVDQL IRSQQAPFIY AMRKATTVIC SRMSPKQKSR VILLMKKEGL CCLAIGDGAN
DVSMIRESSV GVGVKGKEGN AAVNNADYII RKFHHLIKLL FVHGRNNYRG NSYSVYLAFY
ENITFNIPLV ASGSVSHALV LHQLVHDVFG TDDLFFLPAL HALLLHLSHV RLLRILLPGP
HQANAALSSR DLRAQCPYPR FHVST
//
