ID A0A1B9H1S5_9TREE Unreviewed; 1834 AA.
AC A0A1B9H1S5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=P-type phospholipid transporter {ECO:0000256|ARBA:ARBA00012189};
DE EC=7.6.2.1 {ECO:0000256|ARBA:ARBA00012189};
GN ORFNames=I316_01138 {ECO:0000313|EMBL:OCF37231.1};
OS Kwoniella heveanensis BCC8398.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296120 {ECO:0000313|EMBL:OCF37231.1, ECO:0000313|Proteomes:UP000092666};
RN [1] {ECO:0000313|EMBL:OCF37231.1, ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|EMBL:OCF37231.1,
RC ECO:0000313|Proteomes:UP000092666};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus heveanensis BCC8398.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|Proteomes:UP000092666};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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 -!- 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}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109}.
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DR EMBL; KI669493; OCF37231.1; -; Genomic_DNA.
DR STRING; 1296120.A0A1B9H1S5; -.
DR Proteomes; UP000092666; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000092666};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1240..1261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1267..1284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1314..1335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1355..1373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1380..1399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1419..1439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 226..270
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1200..1449
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1470..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1701..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1743..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1701..1723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1834 AA; 202073 MW; AA95335348B1ADD1 CRC64;
MAAASSSHPF DPYAPSSSTY SLDPSSSTAQ LNPHSDAPNH GYAHGQGQPP ARSYLNVNDS
EEEEDLFDPE SIDPSSIDPE LRLRTVKTAH SVIAESIRSE AAAENRRAKK RHLFRSMRRK
ASGITTSSRK KKAASTAASD TEPGSLDSRR DTVTTIGSEF GNANLQQQQQ PLPPASTAPS
TPEQLPADKA TGKKGKGKSP APRRSVFVNI PLPTSLLNMK GDPIIRYVRN KVRTSKYTII
TFLPKNIFEQ FRRVANIYFL FLVIIQLFSV FGAPNAQIGM LPLIFILGMT AIKDGIEDWR
RAQLDNEVNN SATTKLGGWR NVNQPKDPRS FFEKLFNIGP APGRPSKGVR NLREREGSDG
NQIVMENRKD TDGTEQLEDD VVIVDKESYP LSTMPSAAIP SLSITGPQDD VQGSYRQSLM
LKKTSSMPSM ISRRSVGVVD WNFPASGSAQ WERTLWKKLE VGDLVLLRDN EQVPADIIVL
STSNADNLCF VETKNLDGET NLKIRRGLKA TASINSEEDL EHAKFVIDSE PPHANLYTYN
GVLRYTPADA YDKGEEKAEG ITINELLLRG CSLRNTKWVI GMVVFTGGDT KIMLNGGDTP
SKRSKIEKET NFNVIMNFVV LLVLCLITAI LHGWYRSLSG TSAEYYEPGA EAAENIYLDS
VIIFFSCLIV FQNIVPISLY ITVEVVKTVQ AYFIFQDVEM YYEPYDTPCV PKTWNISDDL
GQIEYVFSDK TGTLTQNVME FKKCSIQGVP FGEGMTEAMM GAAKRDGQET GPAMEDQEVE
LDALKKKMLD MMKHTINNRY LREDKLTLVA PDLVSKMANP SDPLRPHIIN FFRALAVCHS
VLSDTPEPSK PFELEYKAES PDEAALVAAA RDVGFPFINK NTNSLDIEVL GNPERWTPLR
LLEFNSTRKR MSVIARGPDG RILLFCKGAD SVIYGRLDPN HDEALKQATL KDLETFANGG
LRTLCIAYRE MSEAEFAEWS KKYDAAAAAT VDRDGEIEKA CELVEHSLTI LGATALEDKL
QEGVPDAIAT LHRAGIKLWI LTGDKLQTAI EIGYSCNLLT NDMEVMIISA DSEEGARAQI
EAGLNKIASV IGPPPTTSGG KIINPGMNTS ATFAVVIDGE SLRYALQPNL KSLFLNLGTQ
CSAVICCRVS PSQKALTVRL VKEGCNAMCL SIGDGANDVA MIQEANVGVG LYGLEGSQAA
MSADYAFGQF RFLTRLLLVH GRWSYVRVAN MHANFFYKNA IFTICMFWYL IFCSFDATYI
FEYTLLLGFN LIFTSLPVGV MGIFDQDVNA KAAAAFPQLY KRGIAGLEYT RTRFWLYMFD
GLYQSAVIFF IPWAVYGQGE TWSSSGRDTN CLHDLGTTIA CAGVLAANSY VGINNRYWTV
ITWVIIGLST LLVYIWIPIY SSLAVLPYAG EATIIYPTFT FWSTILLTWA IAVGPRWFVS
AFKQSYMPKD KDIIREAWIS GELKRELGLK RRRDKKKSKG GLNDQDTSSV PQPKKRGSVI
DHFQKAYGGF SDDTRGQYEP ALTFSPQKDF SRSPMMSDDE GGTGTHTPRS MFSYPPSPAP
PHQLISTHNS PTPGPRNIGT VPPPLLLRHS SEPGPYSPMS DSLSPGLEAP SFGNRQLETP
VSRLSYTSPS VFDTMSHAEA EINREVRRLS RASTEIKRAS LTGGYEISGS NGNAQGSLRG
SRGSLASPIK RLSLPLLGVS VSGATNGQRR DSAVSNSGLM APDLSPIRSS FELEGQDQIQ
NQNHNHKENH DGSRRGVFTS SSHQSQAHDG QVNFASADGG GDQGVWGGSQ RDDQRQVEQE
GRYHPRYGYG QSYASPPPPS SSPRHREGGY GYAV
//
