ID A0A0D2FA97_9EURO Unreviewed; 1236 AA.
AC A0A0D2FA97;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=PV05_05556 {ECO:0000313|EMBL:KIW56944.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW56944.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW56944.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW56944.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) 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; KN847319; KIW56944.1; -; Genomic_DNA.
DR RefSeq; XP_013317528.1; XM_013462074.1.
DR AlphaFoldDB; A0A0D2FA97; -.
DR STRING; 348802.A0A0D2FA97; -.
DR GeneID; 25327464; -.
DR HOGENOM; CLU_000846_3_1_1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000054342; 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; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 2.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 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:UP000054342};
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 207..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 233..250
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 517..536
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1029..1050
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1062..1081
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1111..1129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1141..1160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1167..1188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1200..1221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 175..230
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 999..1227
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1236 AA; 137204 MW; BC2468CBB79F6B9F CRC64;
MSRPNTVHAG GDIDSASEDD LDLDELDPAA TAFLNGSLGH ASEESKRRLQ GKTGNIPLQR
LQKYGGSRLW RSKGRQKGES AVDEDTEALL NNWPGHSRGK GHIRRWSEER AGWNVRNQRR
QNSIGQNDAS QARETPSRRP SQSMQFQEFV RQELADMRDN KHVDNADSRE IQVGQSQKKR
FPTNVVSNAK YTAWSFLPRT LYNEFSFFLN IYFLLVALSQ IIPYLRIGYM STYIVPLACV
LTITIGKEAV DDIARRRRDA EANSELFTVV SFPDAARPRQ QGVVEVQKRS RDIKVGDVLK
LEKNQRVPAD VVILQSHLTE LHSELTTNEA GDGVASASDT GETFIRTDQL DGETDWKLRL
PSPLSQNLKL SELQRLQITA GAPDKQVNHF VGTLDLRSNQ SSAYDPHPSE QDLVHDAPDS
SNQDELHTNR SSSAPLTIDN TAWANTVLAS STTTYCVVVY TGRQTRSALS TSPSRSKTGL
LELEINNLTK ILCIMTLTLS IVLVALEGFE PSNKKPWYVA IMIYLILFST IIPISLRVNL
DLGKSVYANF IEHDKGIPDT VVRTSTIPED LGRIEYLLSD KTGTLTQNEM LLKKIHVGTV
AYSGDAMEEV AAYIDQAFSS TDDTDSQGAT TTKTRREIGV RVRDLILALA LCHNVTPTTD
EVDGERVVSY QASSPDEIAI VEFTESVGLR VLHRDRENIV LQSVKSDRIV LRAEIKDIFP
FTSDSKRMGI IVQLSSEIPG ITSMAGDELW FFQKGADTVM SSIVAANDWL DEETANMARE
GLRTLVVGRK RLSPSQYAEF SSAYTDASLA LHERDAGMAS VVQAHLEHDL ELLGVTGVED
RLQKDVKPSL ELLRNAGVKI WMLTGDKIET ARCVAVSARL VARGQHIQTM ARLKTKAQAK
DALDLMRNQT ESCLLIDGET LALVLAQFRL DFITIAVQLP AVIACRCSPT QKAEVAHLIR
KHTKKRVCCI GDGGNDVSMI QAADVGIGIV GKEGRQASLA ADFSITQFCH LTKLLVWHGR
NSYKRSAKLA QFIIHRGLII SVCQTMYNIA GHFDPKGLFK DWLLVGYATV YTMAPVFSLV
LDRDVDEQLA NLYPELYKEL KSGKSLSYQT FFTWVLVSVY QGIIIQGLTQ LLVGEVDGPR
MLSVSFTVLV LNELIMVAVA VTTWHPIMII CIVGTATLYA ASVPFLGGYF DLAYVASWSW
VWRVVAVGAI SLVPVWGGKA IKRMWKPPNY RKVQGI
//
