ID A0A1E3QM38_9ASCO Unreviewed; 1585 AA.
AC A0A1E3QM38;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=BABINDRAFT_162450 {ECO:0000313|EMBL:ODQ78763.1};
OS Babjeviella inositovora NRRL Y-12698.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ78763.1, ECO:0000313|Proteomes:UP000094336};
RN [1] {ECO:0000313|Proteomes:UP000094336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) 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; KV454434; ODQ78763.1; -; Genomic_DNA.
DR RefSeq; XP_018984091.1; XM_019129359.1.
DR STRING; 984486.A0A1E3QM38; -.
DR GeneID; 30147212; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000094336; 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 GO; GO:0071705; P:nitrogen compound transport; IEA:UniProt.
DR GO; GO:0045332; P:phospholipid translocation; IEA:UniProt.
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; 1.
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; 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:UP000094336};
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 258..275
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 281..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 586..609
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 629..654
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1221..1240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1252..1273
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1303..1322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1342..1361
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1368..1388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1408..1428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 229..280
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1189..1438
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1585 AA; 178159 MW; 4F6676D69143612A CRC64;
MPTPRKPSAR QQSPFEESPY PPIAEQFDNM EFSDMAPNFG GTRPQSLQTD VSDMDSIMKS
PVMDTFEFET GPYASPGSSR VPSGPGLPSR PGPTKATNPY RQTTPKLSDA FERSIEYSEE
PPDASRDPPH IQLHLPDNHT GHEGDTMKRH RWGTQRTKKG KPAGMARSKT LRWKRQTSQK
PLSRRNSTDH VDEDESDDEN DRKNELRTIY FNLPLPDDLL DPSTREPVAT YPRNKVRTTK
YTPLSFVPKN LAFQFKNVAN VYFLILIVMG FFSIFGVPNP AVSAVPLIVI VVITAVKDAI
EDSRRTLLDA EVNNTPTHIL QGVENANTSD DNISAWRRFK KACTRGVVVT FRYFNGVFTK
DGRVQRTRDK EEAARKDAPR KLFQRDSFDS YMSDDRRKSF QMADLSNPFT DSNAVNTILD
PSLPLDTSVR FRKLYWKSVK VGDIVRIHNN DEIPADVAIL ATSDADGACY VETKNLDGET
NLKVRQALKC GGRLQRAADC SRMKFWLESE GPHANLYSYQ GNLKWERGEV SNEAITINNM
LLRGCSLRNT KWAVGIVVFT GTDTKIVLNA GITPTKRSRI TRELNVSVLL NFVLLFVICF
VSGIVNGVYY ARKNESRQFY EFGDIANGAA ANGIVGCFVA VILYQSLVPI SLYISIEIIK
TAQAFFIYSD VLMYYARLDY PCTPKSWNIS DDLGQIEYIF SDKTGTLTQN VMEYKKCTIN
GITYGRAYTE ALAGMRKRQG IDVESEGARE RELIRIDKDV MLEKLHAINR NPQLTEAKVT
FVSSEYVDDL NGAKGGYQQK CNEHFMLTLA LCHSVIAEPS KTDPDKLVYK AQSPDEAALV
GTARDTGFTF LLRTKKGLVV NVQGEDKEYQ ILNTLEFNST RKRMSAIVKI PSANPSEPPK
ALLICKGADS IIYSRLRKDN DQDLLERTAL HLEEFATEGL RTLCIAQREL SWTEYEEWNR
KHEIALAAIT KREEKMEEVA DSIERELILL GGTAIEDRLQ DGVPDSIAIL GQAGIKLWVL
TGDKVETAIN IGFSCNLLGN DMELLVIKTE GEDIARLVDG SQEPKMIVDA LITKYLAKFQ
LQGSMEELVA AKGDHTPPNP NFGVVIDGDA LKLALQGETQ RKFLLLCKQC KAVLCCRVSP
AQKAAVVKMV KETLDVMTLA IGDGSNDVAM IQAADVGVGI AGEEGRQAVM SSDYAIGQFR
FLTRLILVHG RWSYKRLSEM VPCFFYKNVI FSIALFWYGI YNDFDGSYLF EYTYLMFYNL
AFTSIPVVLM GIVDQDVSDV VSLLVPQLYK TGILRSEWTI TKFWWYMGDG LYQSVISFYF
PYLCFYKGFV GMDGLTRDHR FWMGMYVATI AAAACNIYIL FHQYRWDWLL SLLVAVSILL
VFGWTGVWTS FTSSQEFYNA ASQVYGSASF WVCLFVGIMA CILPRFAYDF AQKLYFPKDV
DIVRECVARG DFAAYPLNYD PTDPDRVKIS DYSRGKSMDA PRMSMSSDVS SMVTATVGGT
DLNITRPNRS TMLSGYGSPS LFETYGEGFP EAEARTSLER TRRSMAEERG PMRRSMDRPR
TSLEIPSVTT AVGLIKTLSN GRQVL
//
