ID A0A319BW27_9EURO Unreviewed; 1469 AA.
AC A0A319BW27;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=BO82DRAFT_320917 {ECO:0000313|EMBL:PYH76895.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH76895.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH76895.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH76895.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-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}.
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DR EMBL; KZ821749; PYH76895.1; -; Genomic_DNA.
DR STRING; 1448315.A0A319BW27; -.
DR VEuPathDB; FungiDB:BO82DRAFT_320917; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000248340; 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: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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000248340};
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 484..506
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 526..550
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1103..1119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1131..1152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1182..1203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1223..1241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1248..1268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1288..1308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 103..155
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1068..1317
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 637..664
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1354..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1469 AA; 164340 MW; CC85FBC5FB44A909 CRC64;
MDSYDGKGEN GLERASSEVP PLPSSSEADA NKKSTKRARW ATKRMTAASG LRKRVSILER
GRRQNQTDTM ASATAGVPEI AEGESGSRKV HFNLPIPDEE RDEEGNLKAV YPRNKIRTAI
YTPLTFIPKN LWLQFHNIAN LYFLFVIILQ CFEIFGDADP GLSAVPLIVI VVVTAVKDAI
EDWRRTVSDN ELNNSPVYRL TDWDNVNVTA DNVSVWRKFK KACTRAVITS YRGMKRLFRK
NGADKDVAGD VEMADARPSV EPTSPIAIEM TAVSPTMEAR ASGDWPDPMN DHDQQAYSPW
ARTKGSVVNP KRVTPGKARF KRQHWKDVNV GDFVRLYNGD QIPADIAILS TSDPDGACYV
ETKNLDGETN LKVRNALNCG RVLRNARDCE KAEFTVESPP AHANLYSFSG AIYWDQYDES
GEAPQNRVEP VTINNILLRG CSLQNTEWVL GVVLFTGPET KIMLNQGLTP SKRPQMARNM
NWNVVYNFAI LFIMCVISGF INGFAWGLDD ASLTFFEYGS YGGTPAVQGV IAFFVGVVLF
QNLVPIALYI SLEICRVIQA LYIYYDIHMY YERLKMSCVP RSWNISDDIG QIEYIFSDKT
GTLTQNVMEF KKCTVNGVPY GEAYTEAQLG MQRRQGLVNV EEEAAKARQR ISEARVEMIQ
QLRQLHDNPY LKEENLTFVA PQFAADLGGA SGEAQQQAAI DFMTALALCH TVVTERIPGD
PPQIEFKAQS PDEAALVATA RDCGFTTLGR SGESLILNIM GDERRYTILN ILEFNSTRKR
MSVIVQMPDG TIRLLCKGAD TMIYSRLAPG QQRKLRDATT RDLETFAQEG LRVLCIAERT
IEPEEYREWS VMHDAAAAAI VDREEKLEEV SNAIEQNLYL LGGTAIEDRL QDGVPDTISL
LAEAGIKLWV LTGDKIETAI NIGFSCNLLN NDMQMIVFDA PSDIDMAAKL LDSKLEIFGI
TGSDEELEAA RKDHSPPPQT HALVLDGDTL RFMLDDALRQ KFLLLCRKCK SVLCCRVSPA
QKAAVVEMVK NGLNVMALAI GDGANDVSMI QKADVGVGIA GEEGRQAVMS ADYAIGQFRF
LQRLILVHGR WAYRRLGETT ANFFYKNLVW TFTLFWYSIY DNFDGTYLFE YTYITLVNVA
FTSLPVIFMG IFDQDVDDRV SMAVPQLYMR GIERKEWTQT KFWIYMLDGF YQSVICFFMP
YMLYQVANFQ TENGMGIDDI YRVGVLVATC AVVTSNTYVM MNMYRWDWFS TLINAISSLL
IFFWTGIYSS FESSATFYGA AKQVYGALSF WVVFLLTVVI CLTPRFVCKC IQKVYFPMDV
DIIREKVILG HYDYLKQYEA YVPPDAGKLA GSSESEASAA TSDPENIHQT IVPRHYPGGD
NVDRTANSTP VAPLVDSHGA PTRLDNSQFT SANSSVAFGL QRNTSWDSAS REQSVLSGPV
LPVDSTSMEP QQPHSPLKSR GDPPSTYPV
//
