ID A0A2H9TMI1_9FUNG Unreviewed; 1492 AA.
AC A0A2H9TMI1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=PSACC_01226 {ECO:0000313|EMBL:PJF18947.1};
OS Paramicrosporidium saccamoebae.
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Paramicrosporidium.
OX NCBI_TaxID=1246581 {ECO:0000313|EMBL:PJF18947.1, ECO:0000313|Proteomes:UP000240830};
RN [1] {ECO:0000313|EMBL:PJF18947.1, ECO:0000313|Proteomes:UP000240830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSL3 {ECO:0000313|EMBL:PJF18947.1,
RC ECO:0000313|Proteomes:UP000240830};
RA Quandt C.A., Beaudet D., Corsaro D., Michel R., Corradi N., James T.;
RT "The genome of Paramicrosporidium saccamoebae is the missing link in
RT understanding Cryptomycota and Microsporidia evolution.";
RL Submitted (OCT-2016) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
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:PJF18947.1}.
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DR EMBL; MTSL01000093; PJF18947.1; -; Genomic_DNA.
DR STRING; 1246581.A0A2H9TMI1; -.
DR Proteomes; UP000240830; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF150; 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:UP000240830};
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 179..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 502..521
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1082..1102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1114..1135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1165..1183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1203..1222
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1229..1252
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1268..1287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 149..203
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1051..1296
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1492 AA; 169376 MW; 7E3F89EF7CAAE8FF CRC64;
MPPNSRRYQS PSTLFRRKTR KEGKLRRWKS AASNWLNGLP VTQEDFDSSS IQQELHSSTR
ARRSTRASIK HHLKPKNWFR SRDNSIESDL AMAGTPGPQP NLEDKKEDES VNLVLQEPPV
DERPPVRIIQ LPPEPLAHVP LANKKDDIHS TMVTNEIRTA KYTMLNFLPK NILEQMRRVA
NIYFVFIVFL QCFPAVSNYN PVLAAAPIVI IMVVTAIKDA VEDWKRHKQD NEVNYSIALT
LNRPDGGAIV QRDTRYQRFA NRMIHWRDMT IRAVQILYGK IKRTPVPVSG RHQKLEKLPE
GQVNWKQTFW RDMRVGDIVL LRNNEMIPAD VMILSTSEPD GICFVETKNL DGETNLKIRR
CLYETEWIKR PEDAYNMKAT IEVDLPNNNL YLFNGRIIFS KEIPSPIKQQ EMEEAEEFSG
IPALEDDIDG KAIITRSESA FVEPAVLPVS HEGLLLRGCI LRNTGYVIGV VVYTGPHTKL
MLNSGGTPSK RTRIERQMNP QIILNFILLF IICVSCAIVQ SQFSASADTA PFWVSGFDSG
LLTSPAFLGF LTFWSSLILF QTLVPISMYV VVEIVKTVQV SIHYDLPCQI EYLFSDKTGT
LTQNVMEFRR CSIGGQVYGT LTPSEPGEAV ELSRSSSATM RAAESGKWTT AESEMVTSLQ
QMLTYPYVPP SKFSFVDEHL FTSIREDAEQ REKIFSFFLL LTVCHTVLID RPVDSEEEED
FVKKSDDFKP HNLLFKAQSP DEAALVSAAR DLGFVFLGRD KDFIFVSNLG EIETITVLNV
LEFSSDRKRM STIVRRQNGE IVLMCKGADN IIFERLSQDS LESQVAQLTQ NHLENFAEEA
SAAMHNRELF MDAASDEIER DLTLLGATAI EDKLQEGVPE CIEMLQMAGI KVWVLTGDKM
ETAINIGFSC RLLNKNMVLL VIRGSDEEET LKQLRSAYEK IWSRYFSFGD TSGEQIASNA
TSSFAMIIEG KTLKFALEKS CRKIFVNLSS RCDAVICCRV SPLQKAKVVE LIRHGKNVMT
MAIGDGANDV SMIQAADVGV GIAGQEGMQA VMSSDYAIAQ FRYLTRLLLV HGRWSYIRVA
EVTLLSLYKN LAFVVLLFWY QFYCGFTAQY VYDYMFLLFF NIVFSILPLL ILGSFDRDLT
DKYLLSVAPI YQQGIRQTSY SMKLFIFYLI DALYQSIVCF FIPMLAYSDT AITYSGQTEN
QTLLGNVMAL SIITCTNMYM AINTFSWVAA MFIGLAITII AVFGFVLVYS LIPMQNLYGS
WRNFLDPIFW ATIVLSIVIS QMPRLLAKYV QTIWRPGDLD IVREITKWGF GQADLWRSLI
PIHATMPRLG EVQLEDVIKA PEKAMIRTEP RRILGMELAD EIPIEMEKGK CIEVIEEKPR
HRFLRRSLGM FNLRTGRFER MTGFAFSQED GMGEVVTHNR PRPTKAFGAV FLGDSQAENL
RRVSQIPPVS MGSFTLPTPT VPIAAARRET SRRSNRNSFS LHFPRFSVAK ER
//
