ID A0A6G0XX23_9STRA Unreviewed; 1364 AA.
AC A0A6G0XX23;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=Ae201684_000657 {ECO:0000313|EMBL:KAF0745085.1};
OS Aphanomyces euteiches.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=100861 {ECO:0000313|EMBL:KAF0745085.1, ECO:0000313|Proteomes:UP000481153};
RN [1] {ECO:0000313|EMBL:KAF0745085.1, ECO:0000313|Proteomes:UP000481153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 201684 {ECO:0000313|EMBL:KAF0745085.1,
RC ECO:0000313|Proteomes:UP000481153};
RA Gaulin E.;
RT "Genomics analysis of Aphanomyces spp. identifies a new class of oomycete
RT effector associated with host adaptation.";
RL Submitted (JUL-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:KAF0745085.1}.
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DR EMBL; VJMJ01000003; KAF0745085.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:AeMF1_003121; -.
DR Proteomes; UP000481153; 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:UP000481153};
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 143..162
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 354..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 395..418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 928..949
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 961..985
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1014..1034
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1054..1071
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1078..1101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1113..1132
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 93..141
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 900..1147
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1364 AA; 153439 MW; 802437564B4CB1C3 CRC64;
MSSDLPPTDL IRAAAAVAET QDDAQAEYVA MRDVPTPRAS IPQVQEEHYV AVEESTLSGN
GQWSDVLHSP QSNVGPSNMM EQILKETNTT GPTSNAIRTS HYTWWNFLPV FLYYTFRKMA
NFYFLMIGFL QMIPPISPTG GVPLQFLPLF IVVLIDAIFA IIEDNQRHRA DDVTNNTPCQ
RYNIRTGEFE AVTWKDIIVG DLIQLSDNEI APADLVVLAT DGQMAMDGFG VCYIETKSLD
GEANLKLRES LLQSRFDVPI NEFVEAMRGL KFEHDPPSAD IHSYHGAVHC ITNEEVTTLP
IDVQNTIWRG CKVRNTKRMW GVVAYAGVDT RIMQGLTERD MKQSTIDSVT DAQVVIIVIL
LIALCIIGAS SYTIWSSPSL PHYLGDAINN PFITSFFYFL ITMASILPIT LYVSITTVKA
LQGYFMTRDM EMYDAEHDMH MQARNKALNE QLGHITHIFS DKTGTITCNK MEFRKCSIRG
ISYGTGTTAI GRAAARAISA SGKTEGIDTD ETTFEPIRKA NSVPNVNFHD PRIHEDLKGA
SGADQEESIR EFFRHLALCH SVLIDSSSAF VASSPDELAL VSGAKFFGYE FIERNPGAML
IQAPDGTKES YEILEVFEFT SARKRMSVAL KRKDHVLFLC KGADTILYPR VKEDTWVTDT
QTHLKGYASE GLRTLVIASK VVPLDEWERF YEEYQQLQVN DPTDLERLQD IMERDLTLLG
VTAIEDRLQD QVPETIQLLS KAGIGLWVLT GDMEETAINI GYACSLLTNT MERYVINAKT
CPTRICLLQR LDEIYNRMIY SAFGGQDLAI IIDGASLHLI LNEDPEHVDG LHFLRVALLC
RVVIACRCSP IQKAQLVDLV QKNCDDARTL AIGDGANDVP MIRAAHVGIG IAGEEGRQAV
NQSDFAIGQF RFLARLLLVH GRWNYNRIAY LIFFTYYKNI VYCMSMFWYM LTYSAYSGTL
VYAVFIQQGY NLFFTCLPII AFAVLDQDVP ADVAMALPQL YNLTGRKLFK NSRFWKWVIM
AVIDSVMLLY LLTWSSSKID PDGSTSTLMD LGNLGWTVLC VYMNVRVLLI ISTWNVFVYA
SLIISFALIY GLEIAIDYVG LQDPTWMTSF PRMFGQGNVW LIQLMIIIAL VFKDIMFNAY
QRTFHPTVLD LAQLATTSSS AKRGASSGMP TLESLTSIEF PYVKWILPHL HNLANNEETS
DAEPAENIRQ SGYHGFAFDE PVHAIRWLMT RKHSHVAKPK HSRWNTEFLQ FILSTSDPVV
YENERYQPFL GFGHTFPGHL LPSDRGHWSN ASGAISTNKE ISTAVLRVDM SLPNCDRDGW
VYASDFSRFP SGTCARTFAL VRRRRWVLRE AASTISDPDS PPPM
//
