ID A0A4Q9PYY3_9APHY Unreviewed; 1144 AA.
AC A0A4Q9PYY3;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, 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=BD310DRAFT_1038121 {ECO:0000313|EMBL:TBU60017.1};
OS Dichomitus squalens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=114155 {ECO:0000313|EMBL:TBU60017.1, ECO:0000313|Proteomes:UP000292082};
RN [1] {ECO:0000313|EMBL:TBU60017.1, ECO:0000313|Proteomes:UP000292082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 464.89 {ECO:0000313|EMBL:TBU60017.1,
RC ECO:0000313|Proteomes:UP000292082};
RG DOE Joint Genome Institute;
RA Lopez S.C., Andreopoulos B., Pangilinan J., Lipzen A., Riley R.,
RA Ahrendt S., Ng V., Barry K., Daum C., Grigoriev I.V., Hilden K.S.,
RA Makela M.R., de Vries R.P.;
RT "Draft genome sequences of three monokaryotic isolates of the white-rot
RT basidiomycete fungus Dichomitus squalens.";
RL Submitted (JAN-2019) 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; ML145108; TBU60017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q9PYY3; -.
DR STRING; 114155.A0A4Q9PYY3; -.
DR Proteomes; UP000292082; 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; 3.
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; PF00702; Hydrolase; 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:UP000292082};
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 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 409..428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 434..453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 944..964
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 970..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1022..1042
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1048..1069
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1076..1095
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1110..1128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 133..184
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 910..1137
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1144 AA; 128223 MW; C84FF8091B52F9B9 CRC64;
MSEIPLHTFG RTRKSRAGYT PLHNGEPSDE VHGNGTNGLG PDNSNGRTMH GVVRAAVASS
GSVNRKGQRR ERYADDPEEE ETLLGDASHE DGGFRNDEPE EQIRETSQRS TSSRRGKSSD
KSRIIPFRPP EKLQGKYPPN VVRNQKYNVF TFLPLVFYEQ FKFFFNLYFL LVALSQFIPA
LKIGFIVTYI APLAFVLTVT MGKEAYDDYK RNLRDREANS QKYLVLDPSE YSESSPEGIP
YTRSVPSSSL RVGDLVVLEK NQRVPADLVL LRTSDSSGTC FIRTDQLDGE TDWKLRVAVP
ACQKLSSDRE LLTVDAEIYA DAPIKDIHTF IGTFTINSPP SLLEDDVPMV QVPTVEPLTA
ENMLWSNTVL AAGSAVGFVI YTGSETRAVM NTSHPETKVG LLDVEINRLA KILCAVTFAL
SLVLVALNGF RGPWYIYVFR FLILFSSIIP ISLRVNLDMG KTVYAQQIMT DNEIPNTIVR
TSTLPEELGR IEYLLSDKTG TLTQNEMEMK KLHMGTVSYG YDSMDEIAHQ LAVAFGSGDE
HGHGRHPSLQ TGVQLATRGR RDMSSRVHDV VLSLALCHNV TPVYNDDGTV TYQASSPDEV
AIIKWTESVG LRLTFRDRTR IELQTPTGAR ISFDVLDIFP FTSESKRMGI IVRDAQTGEI
TFLQKGADVV MTKIVQRNDW LEEECANMAR EGLRTLVMAR RRLSDQSYNH FKEQHHLASI
KLEGRNEAMA AIVAELLEHD LELLGLTGVE DKLQDEVKST LELLRNAGIK IWMLTGDKIE
TATCIAISTK LVARNQYIHQ VAKLKTSDQV RDQLEFLQQK LDCCLVIDGE SLQLCLNMFK
NEFVEIATKL SAVVACRCSP TQKADVARLI RKHTKKRVCC IGDGGNDVSM IQAADVGVGI
VGKEGKQASL AADFSVTQFS YLTKLLLWHG RNSYRRSAKL AQFVIHRGLI ISVMQAVFSS
IFYFAPIALY QGWLMVGYAT AYTMAPVFSL VLDRDVNEDL ALLYPELYKE LTKGRVLSYK
TFFIWLMISV YQGAAIMIMS LVLFENEFLN IVSISFTALI LNELIMVALE ITTWHIYMVV
SEIVTLFIYA ISMTFLPEYF DLTFVLSSRF AWKVAVIVAI SAFPLYIIKF IRSRVAPAAS
SKLL
//
