ID A0A4S3JPN5_9EURO Unreviewed; 1358 AA.
AC A0A4S3JPN5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=ATNIH1004_001317 {ECO:0000313|EMBL:KAA8652413.1},
GN EYZ11_002875 {ECO:0000313|EMBL:THC97649.1};
OS Aspergillus tanneri.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1220188 {ECO:0000313|EMBL:THC97649.1, ECO:0000313|Proteomes:UP000308092};
RN [1] {ECO:0000313|EMBL:THC97649.1, ECO:0000313|Proteomes:UP000308092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH1004 {ECO:0000313|EMBL:THC97649.1,
RC ECO:0000313|Proteomes:UP000308092};
RA Mounaud S., Singh I., Joardar V., Pakala S., Pakala S., Venepally P.,
RA Hoover J., Nierman W., Chung J., Losada L.;
RT "The genome sequence of a newly discovered highly antifungal drug resistant
RT Aspergillus species, Aspergillus tanneri NIH 1004.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA8652413.1, ECO:0000313|Proteomes:UP000324241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH1004 {ECO:0000313|EMBL:KAA8652413.1,
RC ECO:0000313|Proteomes:UP000324241};
RA Mounaud S., Singh I., Joardar V., Pakala S., Pakala S., Venepally P.,
RA Chung J.K., Losada L., Nierman W.C.;
RT "The genome sequence of a newly discovered highly antifungal drug resistant
RT Aspergillus species, Aspergillus tanneri NIH 1004.";
RL Submitted (AUG-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 -!- 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:THC97649.1}.
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DR EMBL; QUQM01000002; KAA8652413.1; -; Genomic_DNA.
DR EMBL; SOSA01000068; THC97649.1; -; Genomic_DNA.
DR STRING; 1220188.A0A4S3JPN5; -.
DR VEuPathDB; FungiDB:EYZ11_002875; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000308092; Unassembled WGS sequence.
DR Proteomes; UP000324241; 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 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; 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:UP000308092};
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 497..520
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 547..568
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1099..1121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1142..1166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1178..1195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1207..1230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1250..1269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 234..300
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1028..1280
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1358 AA; 152532 MW; 9904CFA4727C998F CRC64;
MASGRPPGHH PAAGRDDDLL QLEEPAPMYN SGQGPPVNDE HLLRQFNIND SDQPQARPSI
SYDHFVGGQA PPPLVGAHAM TTAHPPAPSG PYLNDPYMGA EASRTYSQTS GLNNYRRYSI
DDYADEPGYY NLDDGDDPMH TGHRVRQTKE RNSIMGLGGG LMGRAKHMLG MGPDYSEMDL
PLTEAGARAA RVDSAEPDET AAPQHDRRKP KKPGFKFGFG RRKVDPSTLG PRMIMLNNPP
ANAVHKFVDN HVSTAKYNIF TFLPKFLFEQ FSKYANLFFL FTAVLQQIPN VSPTNRYTTI
GPLLIVLLVS AIKELVEDYK RRSSDKSLNF SRTQVLKGSA FHDTKWIDVA VGDIVRVESE
QPFPADLVLL ASSEPEGLCY IETANLDGET NLKIKQAIPE TAHLVSPADL SRLSGRIRSE
QPNSSLYTYE ATLTMHAGGG EKELPLAPDQ LLLRGATLRN TPWIHGIVVF TGHETKLMRN
ATATPIKRTA VERMVNIQIL MLVGILITLS VISSVGDLII RQTASDRLSY LDYGNTHPAK
QFVLDIFTYW VLYSNLVPIS LFVTIEIVKY AQAFLINSDL DIYYEKTDTP ATCRTSSLVE
ELGQIEYIFS DKTGTLTCNM MEFKQCTISG VQYGEDIPED QRATVEDGVE VGVHDFKRLR
ENLQSHPTAD AIHHFLTLLA ICHTVIPERN DEKPDVIKYQ AASPDEGALV EGAAQLGYRF
TNRRPRSVII TVAGQEYEYE LLAVCEFNSS RKRMSTIFRC PDGRIRIYTK GADTVILERL
NPDNPMVEAT LQHLEDYASE GLRTLCLAMR EVPEEEFQQW YQIYDKAATT VSGNRADELD
KASELIEKDL FLLGATAIED RLQDGVPDTI HTLQTAGIKV WVLTGDRQET AINIGMSCKL
ISEDMTLLVV NEETAPATQD NLSKKLQAVQ SQGASGEMEA MALVIDGRSL TYALEKDMEK
LFLDLAVMCK AVVCCRVSPL QKALVVKLVK RHLKSLLLAI GDGANDVSMI QAAHVGVGIS
GVEGLQAARS ADVSIAQFRY LRKLLLVHGA WSYHRISRVI LYSFYKNIAL YMTQFWYSFQ
NAFSGEVIYE SWTLSFYNVF FTVLPPFAMG ICDQFISARL LDRYPQLYQL GQKGMFFKRH
SFWSWIANGF YHSLLLYIVS QLIFLWDLPQ ADGKVAGHWV WGSALYTAVL ATVLGKAALI
TNIWTKYTFI AIPGSMVIWL GFLPAYGYAA PAIGFSTEYY GTIPRLFKSP VFYLMAVVLP
CICLLRDYAW KYAKRMYYPQ HYHHVQEIQK YNVQDYRPRM EQFQKAIRKV RHVQRMRKQR
GYAFSQADEG GQMRVVNAYD TTRGRGRYGE MTSSRALV
//
