ID A0A150V2J9_9PEZI Unreviewed; 1241 AA.
AC A0A150V2J9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
DE Flags: Fragment;
GN ORFNames=M433DRAFT_47805 {ECO:0000313|EMBL:KYG44758.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG44758.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG44758.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG44758.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG44758.1}.
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DR EMBL; JPDO01000205; KYG44758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150V2J9; -.
DR STRING; 766039.A0A150V2J9; -.
DR Proteomes; UP000075602; 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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF174; PHOSPHOLIPID-TRANSPORTING ATPASE DNF3-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_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:UP000075602};
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 347..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 389..410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1096..1117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1129..1149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1156..1173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1204..1222
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 49..106
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 981..1227
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KYG44758.1"
FT NON_TER 1241
FT /evidence="ECO:0000313|EMBL:KYG44758.1"
SQ SEQUENCE 1241 AA; 138946 MW; 4EA24A1E4B816924 CRC64;
RSIKILFLSM YEHYILELLL RQTPLPPSKD GRHIPIRAFR DAPLVDERTA HSYVSNSIRS
ARYTIWDFLP KQFFFQATRL SNFYFICIGV PQAIPGLSTT GNYTTILPLC FFILLTIFKE
GYDDFRRHRL DNVENNQMAT VSGYQSSSSI ATSAKSTIWK ILVSFLAGDQ GKAGAQEQEG
QTVGKDVDDN LGWFKVRWKD IKVGDIVMLQ RDESVPADVV LLYADGENGL AYIETMALDG
ETNLKSKQAP EALRCCATLH GLKECDAEVV SEDPNRNLYD YNGRVVVGGK SIPLTLNEVI
FRGSVLRNTG FAICLVINTG EECKIRMNAN HHPKAKKPHL ERYANQVVLT LIVYVVLLSV
GLSMGYIIWH QNFEVHAWYL NNSYVSFKQI IIGYLIMFNN VIPLALYISL EIVKIGQMLM
ISSDLEMYDA KTNVAMTCNT NTILENLGQV GYVLSDKTGT LTENVMRFRK MSIAGIALVH
ATNNDPKAAI DGGGNASITI ENRRLSRTGM SQNESRLSFA RSRSTFRTPD PTIDLTTADM
ISHMRRQPSS NFSKKARSFI LGMALCHTAL PETGACGDTT FQASSPDELA LLKAAQDLGY
LMIQRSSNSV TLLIREGAEQ ARLVYEVLDI VEFSSKRKRM SIIVRCPDER IWLICKGADN
VIIPRLQQAS MACRTSREVR RSLQLERDMQ RRSASTGPRH NFGDLPSLIM RVHTRSLEVE
DMSARRPSIF FDSPATEDDG IVFSRCFRHL DDFAKEGLRT LLFADKFLLP SEYSCWKKVF
SDASTSLINR QRHIEAAADM MEQGLSLLGA SAIEDKLQIG VPETIDKLRR ANIKIWMLTG
DKRETAINIA NAAQICKPES EIWVLDASKG DLESQLSDAA SDIFRDGGLC HTVLVVDGQS
LASIELNAGL KQTFYSIIVE VDSVICCRAS PAQKAGIVRA IRARLPLALT LAIGDGANDV
AMIQASHVGV GISGKEGLQA ARVADYSIAQ FRFLQRLLLV HGRWNYVRTA KFILHTFWKE
MFFYMMQALY QRSNGYTGTS LYENWSLTVL NTLFTSLCVI VPGIFEQDLK ADTLLAVPEL
YVYGQRNMGL HLSKTIAWII LAAAEGMIVW FISWAAFDVF HKTGDNGLFA LGDLCFSLGI
VWTNLKLLLL ETHYKTAIVG GSFMITFAGW WAWNGFMSSV YEDNLSPYDV KGGFTSTFGN
DPNWWLTMVI VLAVLTSLEI LYKSLAQSSA MVNIFVPWKR W
//
