ID A0A430Q9B2_SCHBO Unreviewed; 695 AA.
AC A0A430Q9B2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=DC041_0007463 {ECO:0000313|EMBL:RTG84254.1};
OS Schistosoma bovis (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6184 {ECO:0000313|EMBL:RTG84254.1, ECO:0000313|Proteomes:UP000290809};
RN [1] {ECO:0000313|EMBL:RTG84254.1, ECO:0000313|Proteomes:UP000290809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAN1997 {ECO:0000313|EMBL:RTG84254.1,
RC ECO:0000313|Proteomes:UP000290809};
RA Oey H., Zakrzewski M., Gobert G., Gravermann K., Stoye J., Jones M.,
RA Mcmanus D., Krause L.;
RT "Genome sequence of the bovine parasite Schistosoma bovis Tanzania.";
RL PLoS Pathog. 0:0-0(2019).
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:RTG84254.1}.
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DR EMBL; QMKO01002224; RTG84254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430Q9B2; -.
DR STRING; 6184.A0A430Q9B2; -.
DR Proteomes; UP000290809; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_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 NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF212; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 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:UP000290809};
KW Translocase {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 305..326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 338..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 388..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 450..473
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 493..516
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 274..527
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 578..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 79598 MW; 8274C4714CB12EA7 CRC64;
MEQPNTFSAY GDPLGDSFCG TAGLKLRMDS EQVMKQVTEF ATLGLRTLVM GIRLITIKKW
NELKTKLDKA RSIVNEGRQK ELITAYNEIE KKLTLIGCTG IEDMLQEGVP ETIRALREAG
IKIWVLTGDK EETAVNISYA AGHFYPGMQE IRVTNFDDTV KCGSFLKSQI ERIKESKIYD
ADTQFGVVID GQSLNYALVE PIRSLFTQCC LESSTVLCCR STPLQKAEVI RLIKESRKTI
PITAAIGDGA NDVSMILEAH IGFGIYGKEG RQAVRASDYA FGRFHYLKNV LLVHGHLYYQ
RVSLLVLYFF YKNLIFTLPQ MLYSFYCVYS QQSIYPQIYL ILFNLIMTSL PIFLYGIFEI
SIPITILLEF PILYQNIARN YILSKKHFLI WISLACWHAF IIFFGTYFLS FQGHANDHGH
SKLSNLICFG NFIILIIFLV VNIKVLLISY YLNWIILLIW NLAIIINISI FLICNNVLFP
TELGKQLYGT YTIMFTGSGC GLIWFSIFCI TLLALIPDLI IRTIDDQNWQ WKLNHLRDEL
KKKQRESKMH TRTSIRNIYD YTNQIVGELQ SHQIDDKSMY SLPNNTSTNK PSMTYNDDDD
DKPTNILNVY NVVSSDTNAL TTTNLNHINT STIPTIFNNN NNNNNNTIHN PKRYSLTNHV
TMPNPIQINS NALNVPRLYE NNVDTLNDNN LLTRF
//
