ID A0A5M6BVR0_9TREE Unreviewed; 1114 AA.
AC A0A5M6BVR0;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=CI109_004710 {ECO:0000313|EMBL:KAA5526934.1};
OS Kwoniella shandongensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1734106 {ECO:0000313|EMBL:KAA5526934.1, ECO:0000313|Proteomes:UP000322225};
RN [1] {ECO:0000313|EMBL:KAA5526934.1, ECO:0000313|Proteomes:UP000322225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12478 {ECO:0000313|EMBL:KAA5526934.1,
RC ECO:0000313|Proteomes:UP000322225};
RA Cuomo C., Billmyre B., Heitman J.;
RT "The Genome Sequence of Kwoniella shandongensis CBS 12478.";
RL Submitted (AUG-2017) 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}.
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:KAA5526934.1}.
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DR EMBL; NQVO01000023; KAA5526934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5M6BVR0; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000322225; 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; cd07541; P-type_ATPase_APLT_Neo1-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:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 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; 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:UP000322225};
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 145..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 380..399
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 405..424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 912..935
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 941..960
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 990..1010
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1016..1037
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1044..1066
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1078..1096
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 92..147
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 878..1105
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 123347 MW; 4BE2214E93252EA1 CRC64;
MSVQTAPSSG ASRAKLGVGH GKGKKKRVSD ADEEEEALLG NGLGGSGGDD DFSFDRMQRD
GGITLGDEGS ISSRPPKTRD KSRTIPLQPV SSKSPFPPNV VRNQKYTILT FLPLVFYEQF
KFFFNFYFLV VALSQFVPAL KIGYIVTYVA PLAFVLAVTM GKEAYDDYSR YLRDREANST
RYLVLLPQPP SPLPTHSNLP LINEDDVPTH RHTPSLPRPQ TRSTPASSIK VGDMVLLEKN
QRVPADMVLL TTSEEEGTCF IRTDQLDGET DWKLKVAVGE TQKMGEKGVG SAEGSLYADP
PIKDIHTFYG VLSLRSTSPG PQTETSYPLS VENILWANTV LAAGSAVGLV VYTGKETRAV
LNTSEPETKM GTLEKEVNRM AKILCTVTFA LSVFLVALNG FRGQWYIYVF RFLILFSSII
PISLRVNLDM GKTVYAHQIH TDKEIPETIV RTSTLPEELG RVEYLLSDKT GTLTRNEMEL
KKLHMGTLVF GWDSMDEVAH LLVTALGEQE SNGRRQNSLP TSNLRGRRDM SSRVRDAVIA
LATCHNVTPV TNDDGTVTYQ ASSPDEVAIV QWTESVGLTL VARDRGSMTL RATSGTEYPF
DILAIFPFTS ESKRMGIIVR DRTTGVITFV QKGADVIMSK IVQKNDWLDE ECGNMAREGL
RTLVLGRKKL SDDGYAEFDR QYRAAQLSSG EERADKVQQV ISTHLESEVE LLALTGVEDK
LQEDVKSTLE LLRNAGLKIW MLTGDKIETA TNIAVSSKLV GRGQYIHQVA KLKTPDQVRD
MLDFLQAKLD CCLVIDGESL QLCLDRFKTE FIILATQLPA VVACRCSPTQ KADVARLIRE
FTKKTVCCIG DGGNDVSMIQ AADVGVGIVG KEGKQASLAA DFSINQFSYL TKLLLWHGRN
SYKRSAKLSQ FVIHRGLIIA VIQAVFSSIF FFAPIALYQG WLQVGYATLY TMAPVFSLVL
DRDVNEDLAL LYPELYKDLT KGRSLSYKTF FTWLTISVYQ GGIIMLLSLL LFESEFLHIV
AISFTALVIN ELIMVALEVT TWHSYMVLSE LGTALVYFGS MAFLPAYFDL SFVLSRTFAT
KVAVIVAVSS FPLYAIKATH RRLNPAAYTK VAGI
//
