ID A0A024GSU1_9STRA Unreviewed; 1538 AA.
AC A0A024GSU1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=BN9_113090 {ECO:0000313|EMBL:CCI49856.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI49856.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI49856.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI49856.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) 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:CCI49856.1}.
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DR EMBL; CAIX01000351; CCI49856.1; -; Genomic_DNA.
DR STRING; 65357.A0A024GSU1; -.
DR InParanoid; A0A024GSU1; -.
DR OrthoDB; 103847at2759; -.
DR Proteomes; UP000053237; 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:SF214; 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; 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 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:UP000053237};
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 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 403..424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 452..476
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1075..1094
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1114..1139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1159..1181
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1193..1212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1224..1241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1261..1278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 131..194
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1044..1293
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1494..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1538 AA; 173156 MW; 4020B11523A4DABB CRC64;
MSSPRTDFLQ SETVEDVPFE STPRHTQYAL DSSPQNDKSI EPRPANVKES SLPLAPVIHR
KLPTDSSMPL LHLETADSID FDATPNMTIP ILNHECPLNV ADLKGIHSAS NNALLLETKE
SVLPNEAYRH VYLNQPSANS QFEYCDNLVK TSRFTIYNFL PKLLFYEFSK LANAYFLIIS
VMQTIKVISN TGGFPASLPA LSIIVLIDMF FACLEDYKRH KMDHISNELP CEKFDLEQES
FIMSKWHLLH VGDIVKVYNR DPIPADILIL GVKEVDPACP TGICYVETKS LDGETNLKLR
QGVELTYTEI SSTKDIAKLR GLVVCERPNN VIHRFHGTFQ NETGNRKECL STNAIALRGS
TLRNTEFMYG LVINTGPDTK IMMASTSTPM KWSNMEMRLN RQILYICVLM LVLCLTGAVI
SVFWNRENLS SEPGELAWYL YDGDALAIRH PVVQFFVMLV YYFLLLNSFI PVSLYVSMTS
VKFLQSYWMN NDVEMYHEET DTPCQVQTMS LNEELGQIDY IFSDKTGTLT RNIMEFRKCS
INGVAYGVGD TEAGIAAEQR LRDENDTYNG SPAFGKTQGP IDSVSSKQDH RIVKVPFVNY
QDDKIFDAMR LKDHNAQRIF DFFEHLAVCH TVMPERGADG ELRLSASSPD EQALVAAAAC
FGFRFFSRAP GRALVERFDS CVEESGTESA SGNQPVKAQY DILEVLEFNS TRKRMSVILR
NPDGAIQLLC KGADSVMYQR LVSTKDYEIL RMRDVTLEHM EQFAMEGLRT LVIASTIIDP
DVYAKWIVRY RSAINDMKQI ELRRDGESNG IDHLMEEIEV GLEVLGATAV EDRLQDQVPE
TIAKLREASI KIWMLTGDKE ETAINIAFAC RLLAPEMERV IISADTHPDL LSVKRTLKRY
IDEISESEAK AGKSKDHASA CGIIPCRGSP VSNDPECARP LTRIENRPTN LRQNDAFALV
IDGETLELAL EDCPELLIEF VEKTAAVIAC RVSPAQKAQL VRLVRERNPK VRTLAIGDGA
NDVSMIQAAH VGVGISGQEG MQAANSSDYS IAQFKYLRRL LLVHGRWNYI RMGKLILYIF
YKNVVLNLTQ YWYMLLYTGY SGQKFFLEWG LQGYNLFFTA LPILLVSIFE QDVPAYLAYE
YPLLYRIGQE NARFNTKIVW GWLSSCAWES AVISFGTVYG TRHYNESGAT PSMWVHGCTA
FTIIVLVVNL KLALHQQMWW PVHIPVYIGS VLLWVILAYF ISSGSSVSGA YWKSVFDKTF
LSGSFWVLVP ILTFVALARD IFWKGYTRAF QPSYRHLAQE VHAFNLSHLA DRLLVFPPPT
EIPRDMETVT TLSMSLAEKN HCRKASMRSP VNTAPILRPL GTTHPIPRGS AFSYDAESVM
VESFLATDRC CLSDSQAKKK VIFERHGSLG SLAFQEMSSS DNLGAGKQSS DSPRSSGTLL
RRSSVGKVFR GAQHSFRSAR SLNRISVNSP GRDILTERSR ARSGEARHLL GTSMNRNAEE
ADQEVEQVSD DFEDSLPRTP LRLARRYTLS QLSRQASA
//
