ID A0A1V6QPH9_9EURO Unreviewed; 1360 AA.
AC A0A1V6QPH9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=PENANT_c001G03042 {ECO:0000313|EMBL:OQD91150.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD91150.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD91150.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MDYN01000001; OQD91150.1; -; Genomic_DNA.
DR STRING; 416450.A0A1V6QPH9; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000191672; 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; 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 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:UP000191672};
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 499..522
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 549..570
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1101..1123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1144..1168
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1180..1197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1209..1232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1252..1271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 236..302
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1030..1282
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 914..941
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 52..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1360 AA; 152445 MW; E086586262727AC6 CRC64;
MASGRPPGSH SAAGRDEDLL LDSGPIYNSG QGPPVNDEHL LERYNIDDSD EPYSQARPSV
SYDNFVGSRV PQGATLHNVG PGPAHPPANA GLHSNDPYSS GSRDRTYSQT SGLDNYQRYS
VDDDLDDAHS GYYDLDADDD RIAQSHSVRR ANERNSILGL GGGLMGKAKY MFGMGNSNQY
SEMDLPLTEA GARRATVDSA STQAAPPKPR KKFSASDLNI FKRSKADPST MGPRMIQLNN
PPANAVHKFV SNHVSTAKYN IFTFIPKFLF EQFSKYANLF FLFTAVLQQI PNVSPTNKYT
TIVPLAIVLA VSAIKELVED YKRRMSDRGL NYSKTQVLKG SSFHETTWVD VVVGDVVRVE
SEQPFPADLV LLASSEPEGL CYIETANLDG ETNLKIKQAI PETAHLVSPS DLSRLSGRVR
SEQPNSSLYT YEATLTMNAG GGEKELPLAP DQLLLRGATL RNTPWIHGIV VFSGHETKLM
RNATATPIKR TAVERTVNIQ ILMLVSILIA LSVISSVGDL VIRQTRSDKL AYLDYGSVQP
VKQFFMDIFT YWVLYSNLVP ISLFVTIEIV KYFQAFLINS DLDIYYDKTD TPATCRTSSL
VEELGQIEYI FSDKTGTLTC NMMEFKQVTI AGIQYGDDVA EDRRATMEDD SEVGIHDFNK
LKENMQSHPS QNAIRELLTL LATCHTVIPE RNGKDPNVIK YQAASPDEGA LVDGAASLGY
RFTNRRPRSV LFEAGGQELE YELLAVCEFN STRKRMSTIF RCPDGKVRIY TKGADTVILE
RLHPDNPTVE ATLQHLEEYA SEGLRTLCLA MREIPEDEFQ QWYQIFDKAS TTVGGNRADE
LDKAAELIEK GLYLLGATAI EDRLQDGVPD TIHTLQTAGI KIWVLTGDRQ ETAINIGMSC
KLISEDMTLL IINEESAEAT RDNLQKKLDA VKSQIASGDA EPLALVIDGR SLTFALEKDM
EKLFLDLAVI CKAVVCCRVS PLQKALVVKL VKRHLKSLLL AIGDGANDVS MIQAAHVGVG
ISGMEGLQAA RSADVAIAQF RFLRKLLLVH GAWSYSRISR VILYSYYKNI TLYMTQFWYS
FQNAFSGEVI YESWTLSFYN VLFTVLPPFA MGIFDQYISA RLLDRYPQLY RLGQEGQFFR
KHSFWAWILN GFFHSLILYI VSQLMFFWDL PMADGKVAGH WVWGEALYTA VLATVLGKAA
LITNVWTKYT FIAIPGSMLL WLIFLPAYGY AAPAIGFSQE YYGTIPVLFK TPIFYLMAVV
LPAICLMRDY AWKYAKRMYY PQQYHHVQEI QKYNVQDYRP RMEQFQKAIR KVRQVQRMRK
QRGYAFSQAD DGGQMRVLNA YDTTRSRGRY GEMASSRPLA
//
