ID A0A319ANT9_9EURO Unreviewed; 1253 AA.
AC A0A319ANT9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=BP01DRAFT_334703 {ECO:0000313|EMBL:PYH48162.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH48162.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH48162.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH48162.1,
RC ECO:0000313|Proteomes:UP000248349};
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; KZ821222; PYH48162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319ANT9; -.
DR STRING; 1450539.A0A319ANT9; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000248349; 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; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 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:UP000248349};
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 213..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 500..519
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1051..1071
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1077..1099
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1129..1147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1159..1178
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1185..1203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1218..1240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 184..233
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1017..1245
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1253 AA; 139490 MW; 78D6AAF7A3729E50 CRC64;
MPSLSEYPHP YGRSSIAGDS GSDDDLDLEE LDPSTTHLYG THRRSREEET QQRSRSPGIA
LRNLRVGVGN RWKRSISGTL GGGQEDTAGL LEDQDRDDGG IRRSHASSRT YTDDDAPLLN
ERRRSSARSL KDAERLSQKS SRFRIPGLKA ARAWFGSSNS TVIEEPNPTE TKPPRDVFVG
QAQRLRYPPN IVSNAKYTPW SFLPRTLYNE FSFFFNIYFL LVALSQIIPV LRIGYMSSYI
APLAFVVSIS LGKEALDDIG RRRRDAEANA EEFTVLSFDR PTGALEVTRR SRDLKVGDIL
KVRKNQRLPA DVVILKSLSN DTAARQSSAL ERPSNLIPAD HGDEPSTSEV NDEASNPSAC
DTFIRTDQLD GETDWKLRLP SLLSQTLSLR EFTRLKITAS APDRRVNEFL GTIELGSSSY
DPHVDKSTHE REQDDQESQP NSAPLTIDNT AWANTVLASN TITYAAIIYT GSQTRAALST
SPSRSKVGLL EYEINNLTKI LCILTLALSI VLVALEGFQP TNDKVWYVAI MIYLILFSTI
IPMSLRVNLD MAKSVYGRFI EKDKDIPGTV VRTSTIPEDL GRIEYLLSDK TGTLTQNEME
LKKIHVGTVS YANEAMEEVT SYVKQSFSGD SLTTPSALFG MQAGSGTAPR TRREIGSRVR
DIVLALALCH NVTPTTDEED GVRVTNYQAS SPDEIAIVRY TEDVGLKLAY RDRQTIVLES
THTGNVVVRA RILELFPFTS ESKRMGIIVQ FETDESILDS SQNENEIWFF QKGADTVMTT
IVAANDWLDE ETANMAREGL RTLVVGRRRL SEQQYAEFTT RYRQASLALQ GRDAGMTKVI
GEYLERDLEL LGVTGVEDRL QRDVKPSLEL LRNAGVKIWM LTGDKVETAR CVAISAKLVA
RGQYIHTVAK VKDKSTAQEA LDFLRNKTDC CLLIDGESLA LMLSQFRSAF ISVAVLLPAV
IACRCSPTQK AEVADLIRHH TKKRVCCIGD GGNDVSMIQA ADVGIGIVGK EGRQASLAAD
FSITQFHHLT KLLVWHGRNS YKRSAKLAQF IMHRGIIISA CQTMYSIASH FDPKGLFINW
LMVGYATIYT SGPVFSLVFD RDVDEELANL YPELYKELKT GRSLSYRSFF TWVLVSVFQG
AVIQGLSQIL LDTITGPRLI SVSFTALVIN ELLMVAIAIT TWHPFMIFSI IGTALVYAAS
VPFLGDYFDL AYIITLDWLW RVVAVSAVAV IPVWAGKLIM RSWSPPSYRK VRG
//
