ID A0A1J9Q5T1_9EURO Unreviewed; 1358 AA.
AC A0A1J9Q5T1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=ACJ73_04763 {ECO:0000313|EMBL:OJD23881.1};
OS Blastomyces percursus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD23881.1, ECO:0000313|Proteomes:UP000242791};
RN [1] {ECO:0000313|EMBL:OJD23881.1, ECO:0000313|Proteomes:UP000242791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI222 {ECO:0000313|EMBL:OJD23881.1,
RC ECO:0000313|Proteomes:UP000242791};
RA Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (AUG-2015) 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:OJD23881.1}.
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DR EMBL; LGTZ01000685; OJD23881.1; -; Genomic_DNA.
DR STRING; 1658174.A0A1J9Q5T1; -.
DR VEuPathDB; FungiDB:ACJ73_04763; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000242791; 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 CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
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; 2.
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; 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 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:UP000242791};
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 496..517
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 544..565
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1096..1118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1139..1163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1175..1192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1204..1225
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1245..1264
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 233..297
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1025..1279
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1358 AA; 152268 MW; 855328BB696BF375 CRC64;
MTSGRPPGYG PPPGNDGNLV QLEDTASVYN TGQRPPVTDD HLLQQFDIQD SDTPQSRPSV
SYDAFVGGSQ PAQAAGGSRP GARPGTGPFY EEGETYRTYS QTADLHNYQR YSDDLNDFDD
ARSAQGYYND QNDLDGAMPV RDARARDRNS ILSLGGGLMG KAKNMLGMGP QYSEMDLPLT
ETGARPARVD TVGADDDGAA PRAQKKFSTG DFKFGSGRRK IDPSTLGPRV ILFNNSPANA
ANKYVDNHIS TAKYNVFTFL PKFLFEQFSK YANLFFLFTA ILQQIPNISP TNRYTTIAPL
AVVLLVSAIK ELVEDWKRKS SDKSLNYSRA QVLKGSSFED TRWINVAVGD IVRVESEQPF
PADLVLLASS EPEGLCYIET ANLDGETNLK IKQAIPETAD LVSPIQLSRL TGRVKSEQPN
SSLYTYEATL TLQAGGGEKE LPLNPDQLLL RGATLRNTPW IHGLVVFTGH ETKLMRNATA
TPIKRTAVER MVNMQILMLV GILLVLSLIS SVGDLVVRMK SADELTYLYI GNVNAAQQFF
SDIFTYWVLY SNLVPISLFV TIEIVKYCHA FLINSDLDIY YDKTDTSATC RTSSLVEELG
QIEYIFSDKT GTLTCNMMEF KQCSIGGIQY AEVVPEDRKV MEGDDSDMGM YDFKQLTKNL
ESHPTQMAIH HFLTLLATCH TVIPERREEK PDVIKYQAAS PDEGALVEGA VMMGYRFTNR
RPKSVIITAN GQEQEFELLA VCEFNSTRKR MSTIFRCPDG KIRIYCKGAD TVILERLHED
NPTVDITLQH LEEYASDGLR TLCLAMREIP DEEFYQWHQI FDKAATTVTG NRAEELDKAA
EIIEKDFFLL GATAIEDKLQ DGVPDTIHTL QTAGIKVWVL TGDRQETAIN IGMSCKLISE
DMALLIVNEE SAQATRENLS KKLQQVQSQA GSPDSETLAL IIDGKSLTYA LEKDMEKIFL
DLAVMCKAVI CCRVSPLQKA LVVKLVKRHL KALLLAIGDG ANDVSMIQAA HVGVGISGVE
GLQAARSADV SIAQFRFLRK LLLVHGAWSY QRISKVILYS FYKNIALYMT QFWYSFQNSF
SGQVIYESWT LSFYNVFFTV LPPFAMGIFD QFISARLLDR YPQLYQLGQK GVFFKMHSFW
SWVGNGFYHS LIAYFLSQVI FLWDLPLTNG KMAGHWFWGT ALYTAVLATV LGKAALVTNI
WTKYTFIAIP GSFIIWMAFL PAYGFSAPRV GAGFSTEYEG IIPNLFPSPV FWLMAVVLPA
VCLVRDFAWK YIKRMYFPQA YHHVQEIQKY NVQDYRPRME QFQKAIRKVR QVQRNRKQRG
YAFSQADEGG QMRVVNAYDT TRSRGRYGEM ASSRPVDL
//
